Calcium in PDB 5w7b: Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
Enzymatic activity of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
All present enzymatic activity of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps:
3.1.1.77;
Protein crystallography data
The structure of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps, PDB code: 5w7b
was solved by
A.Gorelik,
K.Illes,
B.Nagar,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
44.77 /
1.90
|
|
Space group
|
P 21 21 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
109.522,
138.806,
89.530,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
18.5 /
21.3
|
Calcium Binding Sites:
The binding sites of Calcium atom in the Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
(pdb code 5w7b). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 6 binding sites of Calcium where determined in the
Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps, PDB code: 5w7b:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
6;
Calcium binding site 1 out
of 6 in 5w7b
Go back to
Calcium Binding Sites List in 5w7b
Calcium binding site 1 out
of 6 in the Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca601
b:17.4
occ:1.00
|
OD1
|
C:ASP187
|
2.3
|
19.4
|
1.0
|
|
O
|
C:TYR189
|
2.3
|
15.5
|
1.0
|
|
OD1
|
C:ASP183
|
2.3
|
19.3
|
1.0
|
|
OD1
|
C:ASP185
|
2.3
|
21.6
|
1.0
|
|
OD2
|
C:ASP204
|
2.3
|
14.6
|
1.0
|
|
OD1
|
C:ASP207
|
2.4
|
22.7
|
1.0
|
|
CG
|
C:ASP187
|
3.1
|
19.7
|
1.0
|
|
CG
|
C:ASP185
|
3.2
|
20.2
|
1.0
|
|
H
|
C:ASP187
|
3.2
|
22.9
|
1.0
|
|
HA
|
C:ASP207
|
3.3
|
24.4
|
1.0
|
|
H
|
C:TYR189
|
3.3
|
24.7
|
1.0
|
|
C
|
C:TYR189
|
3.4
|
20.4
|
1.0
|
|
CG
|
C:ASP204
|
3.4
|
18.1
|
1.0
|
|
OD2
|
C:ASP187
|
3.4
|
18.0
|
1.0
|
|
CG
|
C:ASP183
|
3.4
|
20.5
|
1.0
|
|
OD2
|
C:ASP185
|
3.5
|
17.0
|
1.0
|
|
HA
|
C:ASP183
|
3.6
|
26.8
|
1.0
|
|
CG
|
C:ASP207
|
3.6
|
23.4
|
1.0
|
|
HB2
|
C:ASP204
|
3.6
|
20.8
|
1.0
|
|
H
|
C:ASP185
|
3.7
|
31.3
|
1.0
|
|
HB2
|
C:TYR189
|
3.8
|
17.2
|
1.0
|
|
N
|
C:TYR189
|
4.0
|
20.6
|
1.0
|
|
CB
|
C:ASP204
|
4.0
|
17.3
|
1.0
|
|
N
|
C:ASP187
|
4.0
|
19.1
|
1.0
|
|
HA
|
C:SER190
|
4.1
|
22.2
|
1.0
|
|
HB3
|
C:ASP204
|
4.1
|
20.8
|
1.0
|
|
CA
|
C:CA602
|
4.1
|
18.6
|
1.0
|
|
CA
|
C:TYR189
|
4.1
|
17.4
|
1.0
|
|
H
|
C:SER186
|
4.2
|
27.1
|
1.0
|
|
CA
|
C:ASP207
|
4.2
|
20.4
|
1.0
|
|
OD2
|
C:ASP183
|
4.2
|
20.4
|
1.0
|
|
CA
|
C:ASP183
|
4.3
|
22.4
|
1.0
|
|
CB
|
C:ASP183
|
4.3
|
20.2
|
1.0
|
|
CB
|
C:ASP207
|
4.4
|
23.0
|
1.0
|
|
CB
|
C:ASP187
|
4.4
|
16.4
|
1.0
|
|
H
|
C:LYS188
|
4.4
|
18.9
|
1.0
|
|
N
|
C:SER190
|
4.4
|
16.1
|
1.0
|
|
H
|
C:VAL184
|
4.5
|
28.2
|
1.0
|
|
CB
|
C:TYR189
|
4.5
|
14.3
|
1.0
|
|
HB2
|
C:ASP207
|
4.5
|
27.6
|
1.0
|
|
N
|
C:ASP185
|
4.5
|
26.1
|
1.0
|
|
OD1
|
C:ASP204
|
4.5
|
17.5
|
1.0
|
|
N
|
C:SER186
|
4.5
|
22.6
|
1.0
|
|
C
|
C:ASP183
|
4.5
|
24.9
|
1.0
|
|
OD2
|
C:ASP207
|
4.6
|
24.6
|
1.0
|
|
HB2
|
C:ASP183
|
4.6
|
24.2
|
1.0
|
|
CB
|
C:ASP185
|
4.6
|
23.4
|
1.0
|
|
CA
|
C:ASP187
|
4.6
|
16.2
|
1.0
|
|
N
|
C:LYS188
|
4.6
|
15.7
|
1.0
|
|
N
|
C:VAL184
|
4.7
|
23.5
|
1.0
|
|
CA
|
C:SER190
|
4.7
|
18.5
|
1.0
|
|
C
|
C:ASP187
|
4.7
|
14.2
|
1.0
|
|
HB3
|
C:ASP187
|
4.8
|
19.7
|
1.0
|
|
O
|
C:ASP207
|
4.8
|
21.1
|
1.0
|
|
C
|
C:ASP185
|
4.8
|
18.6
|
1.0
|
|
CA
|
C:ASP185
|
4.9
|
18.8
|
1.0
|
|
HB3
|
C:TYR189
|
4.9
|
17.2
|
1.0
|
|
C
|
C:ASP207
|
4.9
|
21.5
|
1.0
|
|
Calcium binding site 2 out
of 6 in 5w7b
Go back to
Calcium Binding Sites List in 5w7b
Calcium binding site 2 out
of 6 in the Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca602
b:18.6
occ:1.00
|
O
|
C:VAL212
|
2.2
|
14.8
|
1.0
|
|
OD2
|
C:ASP187
|
2.2
|
18.0
|
1.0
|
|
O
|
C:ASN206
|
2.3
|
19.4
|
1.0
|
|
OD2
|
C:ASP185
|
2.4
|
17.0
|
1.0
|
|
O
|
C:ASP209
|
2.5
|
16.8
|
1.0
|
|
OD2
|
C:ASP204
|
2.6
|
14.6
|
1.0
|
|
OD1
|
C:ASP204
|
2.7
|
17.5
|
1.0
|
|
CG
|
C:ASP204
|
3.0
|
18.1
|
1.0
|
|
HA
|
C:ASP207
|
3.4
|
24.4
|
1.0
|
|
C
|
C:VAL212
|
3.4
|
15.6
|
1.0
|
|
CG
|
C:ASP187
|
3.4
|
19.7
|
1.0
|
|
C
|
C:ASN206
|
3.4
|
21.6
|
1.0
|
|
HB
|
C:VAL212
|
3.4
|
26.1
|
1.0
|
|
CG
|
C:ASP185
|
3.4
|
20.2
|
1.0
|
|
H
|
C:ASP209
|
3.5
|
28.7
|
1.0
|
|
C
|
C:ASP209
|
3.5
|
24.4
|
1.0
|
|
H
|
C:VAL212
|
3.6
|
23.4
|
1.0
|
|
HA
|
C:LYS210
|
3.7
|
25.2
|
1.0
|
|
HB3
|
C:TYR213
|
3.8
|
18.4
|
1.0
|
|
H
|
C:ASN206
|
3.9
|
28.0
|
1.0
|
|
OD1
|
C:ASP185
|
3.9
|
21.6
|
1.0
|
|
OD1
|
C:ASP187
|
4.0
|
19.4
|
1.0
|
|
HB3
|
C:ASN206
|
4.1
|
27.0
|
1.0
|
|
CA
|
C:CA601
|
4.1
|
17.4
|
1.0
|
|
CA
|
C:VAL212
|
4.1
|
20.0
|
1.0
|
|
CA
|
C:ASP207
|
4.1
|
20.4
|
1.0
|
|
CB
|
C:VAL212
|
4.1
|
21.8
|
1.0
|
|
HG12
|
C:VAL212
|
4.1
|
25.4
|
1.0
|
|
N
|
C:ASP207
|
4.2
|
18.8
|
1.0
|
|
N
|
C:ASP209
|
4.2
|
23.9
|
1.0
|
|
N
|
C:VAL212
|
4.2
|
19.5
|
1.0
|
|
N
|
C:LYS210
|
4.2
|
26.0
|
1.0
|
|
HA
|
C:TYR213
|
4.3
|
16.8
|
1.0
|
|
HB3
|
C:ASP209
|
4.3
|
28.6
|
1.0
|
|
CA
|
C:ASP209
|
4.4
|
21.1
|
1.0
|
|
CA
|
C:LYS210
|
4.4
|
21.0
|
1.0
|
|
HB3
|
C:ASP187
|
4.4
|
19.7
|
1.0
|
|
N
|
C:TYR213
|
4.4
|
16.5
|
1.0
|
|
CA
|
C:ASN206
|
4.4
|
17.7
|
1.0
|
|
CB
|
C:ASP204
|
4.5
|
17.3
|
1.0
|
|
CB
|
C:ASP187
|
4.5
|
16.4
|
1.0
|
|
N
|
C:ASN206
|
4.5
|
23.4
|
1.0
|
|
HD2
|
C:TYR213
|
4.6
|
24.6
|
1.0
|
|
CB
|
C:TYR213
|
4.6
|
15.3
|
1.0
|
|
CB
|
C:ASP185
|
4.7
|
23.4
|
1.0
|
|
CA
|
C:TYR213
|
4.7
|
14.0
|
1.0
|
|
C
|
C:ASP207
|
4.7
|
21.5
|
1.0
|
|
CG1
|
C:VAL212
|
4.7
|
21.1
|
1.0
|
|
HB2
|
C:ASP185
|
4.7
|
28.1
|
1.0
|
|
CB
|
C:ASN206
|
4.8
|
22.5
|
1.0
|
|
C
|
C:LYS210
|
4.8
|
21.3
|
1.0
|
|
HB3
|
C:ASP185
|
4.8
|
28.1
|
1.0
|
|
HB2
|
C:ASP187
|
4.9
|
19.7
|
1.0
|
|
H
|
C:SER208
|
4.9
|
30.1
|
1.0
|
|
CB
|
C:ASP209
|
4.9
|
23.9
|
1.0
|
|
HB2
|
C:ASP204
|
4.9
|
20.8
|
1.0
|
|
N
|
C:SER208
|
4.9
|
25.1
|
1.0
|
|
HB2
|
C:TYR189
|
5.0
|
17.2
|
1.0
|
|
HB3
|
C:ASP204
|
5.0
|
20.8
|
1.0
|
|
Calcium binding site 3 out
of 6 in 5w7b
Go back to
Calcium Binding Sites List in 5w7b
Calcium binding site 3 out
of 6 in the Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca603
b:21.0
occ:1.00
|
OE1
|
C:GLU244
|
2.3
|
24.1
|
1.0
|
|
OD2
|
C:ASP222
|
2.3
|
20.6
|
1.0
|
|
OD2
|
C:ASP226
|
2.3
|
18.6
|
1.0
|
|
O
|
C:ILE232
|
2.3
|
24.1
|
1.0
|
|
OD1
|
C:ASN228
|
2.4
|
19.1
|
1.0
|
|
OD1
|
C:ASN230
|
2.4
|
19.8
|
1.0
|
|
CG
|
C:ASN230
|
3.3
|
17.2
|
1.0
|
|
H
|
C:ILE232
|
3.3
|
24.0
|
1.0
|
|
CD
|
C:GLU244
|
3.3
|
26.3
|
1.0
|
|
HD21
|
C:ASN230
|
3.4
|
20.6
|
1.0
|
|
CG
|
C:ASN228
|
3.4
|
17.6
|
1.0
|
|
CG
|
C:ASP222
|
3.4
|
25.6
|
1.0
|
|
HB
|
C:ILE232
|
3.4
|
22.3
|
1.0
|
|
C
|
C:ILE232
|
3.5
|
25.8
|
1.0
|
|
HA
|
C:ASP226
|
3.5
|
30.5
|
1.0
|
|
CG
|
C:ASP226
|
3.5
|
20.5
|
1.0
|
|
H
|
C:ASN228
|
3.5
|
27.8
|
1.0
|
|
HD21
|
C:ASN228
|
3.5
|
20.9
|
1.0
|
|
H
|
C:ASN230
|
3.6
|
20.1
|
1.0
|
|
ND2
|
C:ASN230
|
3.7
|
17.2
|
1.0
|
|
OE2
|
C:GLU244
|
3.8
|
24.9
|
1.0
|
|
HB2
|
C:ASP222
|
3.8
|
27.6
|
1.0
|
|
HB3
|
C:ASP222
|
3.9
|
27.6
|
1.0
|
|
ND2
|
C:ASN228
|
3.9
|
17.4
|
1.0
|
|
N
|
C:ILE232
|
3.9
|
20.0
|
1.0
|
|
HB3
|
C:PRO218
|
4.0
|
28.5
|
1.0
|
|
CB
|
C:ASP222
|
4.0
|
23.0
|
1.0
|
|
HB3
|
C:TRP233
|
4.0
|
28.5
|
1.0
|
|
CA
|
C:ILE232
|
4.1
|
21.0
|
1.0
|
|
HB2
|
C:GLU244
|
4.2
|
30.5
|
1.0
|
|
CB
|
C:ILE232
|
4.2
|
18.6
|
1.0
|
|
H
|
C:SER227
|
4.2
|
27.9
|
1.0
|
|
CA
|
C:ASP226
|
4.2
|
25.4
|
1.0
|
|
OD1
|
C:ASP226
|
4.3
|
23.8
|
1.0
|
|
N
|
C:ASN230
|
4.3
|
16.8
|
1.0
|
|
CB
|
C:ASP226
|
4.3
|
27.6
|
1.0
|
|
N
|
C:ASN228
|
4.4
|
23.2
|
1.0
|
|
H
|
C:CYS229
|
4.4
|
23.8
|
1.0
|
|
OD1
|
C:ASP222
|
4.5
|
22.8
|
1.0
|
|
HA
|
C:TRP233
|
4.5
|
30.7
|
1.0
|
|
H
|
C:GLY231
|
4.5
|
25.8
|
1.0
|
|
HD22
|
C:ASN230
|
4.5
|
20.6
|
1.0
|
|
N
|
C:SER227
|
4.5
|
23.3
|
1.0
|
|
N
|
C:TRP233
|
4.6
|
23.3
|
1.0
|
|
HB2
|
C:ASP226
|
4.6
|
33.1
|
1.0
|
|
CB
|
C:ASN230
|
4.6
|
15.2
|
1.0
|
|
C
|
C:ASP226
|
4.6
|
22.0
|
1.0
|
|
CG
|
C:GLU244
|
4.6
|
29.7
|
1.0
|
|
CB
|
C:ASN228
|
4.7
|
17.6
|
1.0
|
|
N
|
C:CYS229
|
4.7
|
19.8
|
1.0
|
|
HD22
|
C:ASN228
|
4.7
|
20.9
|
1.0
|
|
N
|
C:GLY231
|
4.7
|
21.5
|
1.0
|
|
HG22
|
C:ILE232
|
4.7
|
31.3
|
1.0
|
|
CA
|
C:ASN230
|
4.8
|
19.3
|
1.0
|
|
CB
|
C:TRP233
|
4.8
|
23.7
|
1.0
|
|
CB
|
C:PRO218
|
4.8
|
23.8
|
1.0
|
|
C
|
C:ASN228
|
4.8
|
22.4
|
1.0
|
|
CA
|
C:ASN228
|
4.8
|
18.1
|
1.0
|
|
CA
|
C:TRP233
|
4.8
|
25.6
|
1.0
|
|
HG
|
C:SER227
|
4.9
|
28.8
|
1.0
|
|
CB
|
C:GLU244
|
4.9
|
25.4
|
1.0
|
|
C
|
C:ASN230
|
4.9
|
20.7
|
1.0
|
|
HB2
|
C:PRO218
|
4.9
|
28.5
|
1.0
|
|
HB3
|
C:ASN230
|
5.0
|
18.2
|
1.0
|
|
Calcium binding site 4 out
of 6 in 5w7b
Go back to
Calcium Binding Sites List in 5w7b
Calcium binding site 4 out
of 6 in the Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ca601
b:18.3
occ:1.00
|
OD2
|
D:ASP204
|
2.3
|
14.8
|
1.0
|
|
OD1
|
D:ASP187
|
2.3
|
16.5
|
1.0
|
|
O
|
D:TYR189
|
2.3
|
18.6
|
1.0
|
|
OD1
|
D:ASP185
|
2.3
|
21.1
|
1.0
|
|
OD1
|
D:ASP183
|
2.4
|
19.7
|
1.0
|
|
OD1
|
D:ASP207
|
2.4
|
24.2
|
1.0
|
|
CG
|
D:ASP187
|
3.1
|
22.9
|
1.0
|
|
H
|
D:ASP187
|
3.2
|
27.3
|
1.0
|
|
CG
|
D:ASP185
|
3.2
|
23.5
|
1.0
|
|
HA
|
D:ASP207
|
3.3
|
27.8
|
1.0
|
|
H
|
D:TYR189
|
3.3
|
22.6
|
1.0
|
|
C
|
D:TYR189
|
3.4
|
22.1
|
1.0
|
|
CG
|
D:ASP204
|
3.4
|
23.0
|
1.0
|
|
OD2
|
D:ASP187
|
3.5
|
17.9
|
1.0
|
|
OD2
|
D:ASP185
|
3.5
|
20.2
|
1.0
|
|
CG
|
D:ASP183
|
3.6
|
24.2
|
1.0
|
|
HB2
|
D:ASP204
|
3.6
|
26.8
|
1.0
|
|
HA
|
D:ASP183
|
3.6
|
31.3
|
1.0
|
|
CG
|
D:ASP207
|
3.7
|
27.2
|
1.0
|
|
HB2
|
D:TYR189
|
3.7
|
20.7
|
1.0
|
|
H
|
D:ASP185
|
3.8
|
28.2
|
1.0
|
|
CB
|
D:ASP204
|
3.9
|
22.3
|
1.0
|
|
N
|
D:TYR189
|
3.9
|
18.8
|
1.0
|
|
CA
|
D:CA602
|
4.0
|
19.8
|
1.0
|
|
N
|
D:ASP187
|
4.0
|
22.8
|
1.0
|
|
HB3
|
D:ASP204
|
4.0
|
26.8
|
1.0
|
|
HA
|
D:SER190
|
4.1
|
27.4
|
1.0
|
|
CA
|
D:TYR189
|
4.1
|
23.1
|
1.0
|
|
H
|
D:SER186
|
4.2
|
31.1
|
1.0
|
|
CA
|
D:ASP207
|
4.2
|
23.1
|
1.0
|
|
CA
|
D:ASP183
|
4.3
|
26.1
|
1.0
|
|
H
|
D:LYS188
|
4.3
|
20.1
|
1.0
|
|
OD2
|
D:ASP183
|
4.4
|
21.2
|
1.0
|
|
CB
|
D:ASP207
|
4.4
|
23.1
|
1.0
|
|
CB
|
D:TYR189
|
4.4
|
17.2
|
1.0
|
|
CB
|
D:ASP187
|
4.4
|
18.9
|
1.0
|
|
H
|
D:VAL184
|
4.4
|
32.6
|
1.0
|
|
N
|
D:SER190
|
4.4
|
20.1
|
1.0
|
|
OD1
|
D:ASP204
|
4.4
|
16.8
|
1.0
|
|
CB
|
D:ASP183
|
4.5
|
22.5
|
1.0
|
|
N
|
D:ASP185
|
4.5
|
23.5
|
1.0
|
|
N
|
D:SER186
|
4.5
|
25.9
|
1.0
|
|
HB2
|
D:ASP207
|
4.5
|
27.7
|
1.0
|
|
C
|
D:ASP183
|
4.6
|
26.5
|
1.0
|
|
CA
|
D:ASP187
|
4.6
|
21.4
|
1.0
|
|
OD2
|
D:ASP207
|
4.6
|
24.0
|
1.0
|
|
CB
|
D:ASP185
|
4.6
|
21.7
|
1.0
|
|
N
|
D:LYS188
|
4.6
|
16.8
|
1.0
|
|
N
|
D:VAL184
|
4.6
|
27.2
|
1.0
|
|
HB2
|
D:ASP183
|
4.7
|
26.9
|
1.0
|
|
C
|
D:ASP187
|
4.7
|
15.9
|
1.0
|
|
CA
|
D:SER190
|
4.7
|
22.8
|
1.0
|
|
O
|
D:ASP207
|
4.8
|
29.7
|
1.0
|
|
HB3
|
D:ASP187
|
4.8
|
22.7
|
1.0
|
|
HB3
|
D:TYR189
|
4.8
|
20.7
|
1.0
|
|
C
|
D:ASP185
|
4.8
|
26.1
|
1.0
|
|
CA
|
D:ASP185
|
4.9
|
22.0
|
1.0
|
|
C
|
D:ASP207
|
4.9
|
23.0
|
1.0
|
|
Calcium binding site 5 out
of 6 in 5w7b
Go back to
Calcium Binding Sites List in 5w7b
Calcium binding site 5 out
of 6 in the Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 5 of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ca602
b:19.8
occ:1.00
|
OD2
|
D:ASP185
|
2.2
|
20.2
|
1.0
|
|
OD2
|
D:ASP187
|
2.3
|
17.9
|
1.0
|
|
O
|
D:VAL212
|
2.3
|
15.3
|
1.0
|
|
O
|
D:ASN206
|
2.3
|
19.5
|
1.0
|
|
O
|
D:ASP209
|
2.4
|
22.5
|
1.0
|
|
OD2
|
D:ASP204
|
2.5
|
14.8
|
1.0
|
|
OD1
|
D:ASP204
|
2.6
|
16.8
|
1.0
|
|
CG
|
D:ASP204
|
2.9
|
23.0
|
1.0
|
|
CG
|
D:ASP185
|
3.3
|
23.5
|
1.0
|
|
HA
|
D:ASP207
|
3.4
|
27.8
|
1.0
|
|
CG
|
D:ASP187
|
3.4
|
22.9
|
1.0
|
|
C
|
D:ASN206
|
3.4
|
21.4
|
1.0
|
|
H
|
D:ASP209
|
3.4
|
28.0
|
1.0
|
|
C
|
D:ASP209
|
3.4
|
26.5
|
1.0
|
|
C
|
D:VAL212
|
3.5
|
14.2
|
1.0
|
|
HB
|
D:VAL212
|
3.6
|
26.7
|
1.0
|
|
H
|
D:VAL212
|
3.7
|
23.5
|
1.0
|
|
HA
|
D:LYS210
|
3.8
|
32.0
|
1.0
|
|
OD1
|
D:ASP185
|
3.8
|
21.1
|
1.0
|
|
HB3
|
D:TYR213
|
3.8
|
20.2
|
1.0
|
|
OD1
|
D:ASP187
|
3.9
|
16.5
|
1.0
|
|
H
|
D:ASN206
|
4.0
|
26.4
|
1.0
|
|
CA
|
D:CA601
|
4.0
|
18.3
|
1.0
|
|
HB3
|
D:ASN206
|
4.1
|
28.4
|
1.0
|
|
CA
|
D:ASP207
|
4.1
|
23.1
|
1.0
|
|
N
|
D:ASP207
|
4.2
|
19.9
|
1.0
|
|
N
|
D:ASP209
|
4.2
|
23.3
|
1.0
|
|
N
|
D:LYS210
|
4.3
|
23.8
|
1.0
|
|
CA
|
D:VAL212
|
4.3
|
18.0
|
1.0
|
|
HG12
|
D:VAL212
|
4.3
|
29.8
|
1.0
|
|
CB
|
D:VAL212
|
4.3
|
22.2
|
1.0
|
|
HB3
|
D:ASP209
|
4.3
|
29.3
|
1.0
|
|
HA
|
D:TYR213
|
4.3
|
21.4
|
1.0
|
|
N
|
D:VAL212
|
4.3
|
19.6
|
1.0
|
|
CA
|
D:ASP209
|
4.4
|
22.9
|
1.0
|
|
CA
|
D:LYS210
|
4.4
|
26.7
|
1.0
|
|
CB
|
D:ASP204
|
4.5
|
22.3
|
1.0
|
|
CA
|
D:ASN206
|
4.5
|
18.9
|
1.0
|
|
HB3
|
D:ASP187
|
4.5
|
22.7
|
1.0
|
|
N
|
D:TYR213
|
4.5
|
17.6
|
1.0
|
|
CB
|
D:ASP187
|
4.6
|
18.9
|
1.0
|
|
CB
|
D:ASP185
|
4.6
|
21.7
|
1.0
|
|
C
|
D:ASP207
|
4.6
|
23.0
|
1.0
|
|
N
|
D:ASN206
|
4.6
|
22.0
|
1.0
|
|
HB2
|
D:ASP185
|
4.6
|
26.1
|
1.0
|
|
CB
|
D:TYR213
|
4.7
|
16.8
|
1.0
|
|
HD2
|
D:TYR213
|
4.7
|
23.1
|
1.0
|
|
CA
|
D:TYR213
|
4.7
|
17.8
|
1.0
|
|
HB3
|
D:ASP185
|
4.7
|
26.1
|
1.0
|
|
CB
|
D:ASN206
|
4.8
|
23.7
|
1.0
|
|
C
|
D:LYS210
|
4.8
|
21.5
|
1.0
|
|
H
|
D:SER208
|
4.8
|
29.0
|
1.0
|
|
HB2
|
D:ASP204
|
4.8
|
26.8
|
1.0
|
|
CG1
|
D:VAL212
|
4.8
|
24.8
|
1.0
|
|
HB2
|
D:TYR189
|
4.8
|
20.7
|
1.0
|
|
N
|
D:SER208
|
4.8
|
24.2
|
1.0
|
|
HB3
|
D:ASP204
|
4.9
|
26.8
|
1.0
|
|
CB
|
D:ASP209
|
4.9
|
24.4
|
1.0
|
|
HB2
|
D:ASP187
|
4.9
|
22.7
|
1.0
|
|
H
|
D:ASP207
|
5.0
|
23.9
|
1.0
|
|
Calcium binding site 6 out
of 6 in 5w7b
Go back to
Calcium Binding Sites List in 5w7b
Calcium binding site 6 out
of 6 in the Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 6 of Rabbit Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, S262A Mutant, with Lps within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ca603
b:21.4
occ:1.00
|
OD2
|
D:ASP222
|
2.3
|
26.2
|
1.0
|
|
OD2
|
D:ASP226
|
2.3
|
22.4
|
1.0
|
|
OE1
|
D:GLU244
|
2.3
|
18.4
|
1.0
|
|
O
|
D:ILE232
|
2.3
|
28.7
|
1.0
|
|
OD1
|
D:ASN228
|
2.4
|
20.6
|
1.0
|
|
OD1
|
D:ASN230
|
2.4
|
19.7
|
1.0
|
|
CG
|
D:ASN230
|
3.3
|
18.2
|
1.0
|
|
CD
|
D:GLU244
|
3.4
|
27.6
|
1.0
|
|
HA
|
D:ASP226
|
3.4
|
34.8
|
1.0
|
|
CG
|
D:ASN228
|
3.4
|
20.5
|
1.0
|
|
CG
|
D:ASP222
|
3.4
|
28.1
|
1.0
|
|
HB
|
D:ILE232
|
3.4
|
23.8
|
1.0
|
|
HD21
|
D:ASN228
|
3.4
|
24.5
|
1.0
|
|
HD21
|
D:ASN230
|
3.5
|
21.5
|
1.0
|
|
C
|
D:ILE232
|
3.5
|
31.4
|
1.0
|
|
H
|
D:ILE232
|
3.5
|
29.6
|
1.0
|
|
CG
|
D:ASP226
|
3.5
|
22.2
|
1.0
|
|
H
|
D:ASN228
|
3.6
|
30.1
|
1.0
|
|
H
|
D:ASN230
|
3.6
|
21.9
|
1.0
|
|
OE2
|
D:GLU244
|
3.7
|
27.4
|
1.0
|
|
ND2
|
D:ASN230
|
3.8
|
17.9
|
1.0
|
|
ND2
|
D:ASN228
|
3.8
|
20.4
|
1.0
|
|
HB2
|
D:ASP222
|
3.8
|
33.1
|
1.0
|
|
HB3
|
D:ASP222
|
3.8
|
33.1
|
1.0
|
|
CB
|
D:ASP222
|
3.9
|
27.6
|
1.0
|
|
N
|
D:ILE232
|
4.0
|
24.6
|
1.0
|
|
HB3
|
D:TRP233
|
4.0
|
39.9
|
1.0
|
|
HB3
|
D:PRO218
|
4.0
|
27.6
|
1.0
|
|
CA
|
D:ILE232
|
4.1
|
23.7
|
1.0
|
|
CA
|
D:ASP226
|
4.2
|
29.0
|
1.0
|
|
CB
|
D:ILE232
|
4.2
|
19.9
|
1.0
|
|
HB2
|
D:GLU244
|
4.3
|
33.1
|
1.0
|
|
H
|
D:SER227
|
4.3
|
30.8
|
1.0
|
|
CB
|
D:ASP226
|
4.3
|
22.3
|
1.0
|
|
N
|
D:ASN230
|
4.4
|
18.2
|
1.0
|
|
N
|
D:ASN228
|
4.4
|
25.0
|
1.0
|
|
OD1
|
D:ASP226
|
4.4
|
26.3
|
1.0
|
|
OD1
|
D:ASP222
|
4.4
|
20.5
|
1.0
|
|
H
|
D:CYS229
|
4.5
|
23.7
|
1.0
|
|
HA
|
D:TRP233
|
4.5
|
32.2
|
1.0
|
|
H
|
D:GLY231
|
4.5
|
27.6
|
1.0
|
|
N
|
D:SER227
|
4.6
|
25.6
|
1.0
|
|
HB2
|
D:ASP226
|
4.6
|
26.8
|
1.0
|
|
N
|
D:TRP233
|
4.6
|
25.7
|
1.0
|
|
C
|
D:ASP226
|
4.6
|
23.5
|
1.0
|
|
HD22
|
D:ASN230
|
4.6
|
21.5
|
1.0
|
|
HG22
|
D:ILE232
|
4.6
|
30.7
|
1.0
|
|
CB
|
D:ASN230
|
4.6
|
15.7
|
1.0
|
|
HD22
|
D:ASN228
|
4.6
|
24.5
|
1.0
|
|
CB
|
D:ASN228
|
4.7
|
18.2
|
1.0
|
|
CG
|
D:GLU244
|
4.7
|
25.0
|
1.0
|
|
N
|
D:GLY231
|
4.7
|
23.0
|
1.0
|
|
N
|
D:CYS229
|
4.7
|
19.7
|
1.0
|
|
CB
|
D:TRP233
|
4.8
|
33.3
|
1.0
|
|
CA
|
D:ASN230
|
4.8
|
18.9
|
1.0
|
|
C
|
D:ASN228
|
4.8
|
22.0
|
1.0
|
|
HG
|
D:SER227
|
4.8
|
25.4
|
1.0
|
|
CA
|
D:TRP233
|
4.9
|
26.9
|
1.0
|
|
CA
|
D:ASN228
|
4.9
|
21.4
|
1.0
|
|
C
|
D:ASN230
|
4.9
|
20.2
|
1.0
|
|
CB
|
D:PRO218
|
4.9
|
23.0
|
1.0
|
|
CB
|
D:GLU244
|
5.0
|
27.6
|
1.0
|
|
HB3
|
D:ASN230
|
5.0
|
18.8
|
1.0
|
|
CG2
|
D:ILE232
|
5.0
|
25.6
|
1.0
|
|
C
|
D:GLY231
|
5.0
|
32.5
|
1.0
|
|
Reference:
A.Gorelik,
K.Illes,
B.Nagar.
Crystal Structure of the Mammalian Lipopolysaccharide Detoxifier. Proc. Natl. Acad. Sci. V. 115 E896 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29343645
DOI: 10.1073/PNAS.1719834115
Page generated: Mon Jul 15 13:03:44 2024
|
