Calcium in PDB 5w7f: Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
Enzymatic activity of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
All present enzymatic activity of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A:
3.1.1.77;
Protein crystallography data
The structure of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A, PDB code: 5w7f
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)
|
46.22 /
2.80
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
81.797,
88.354,
93.450,
90.00,
103.01,
90.00
|
|
R / Rfree (%)
|
21.6 /
26.5
|
Calcium Binding Sites:
The binding sites of Calcium atom in the Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
(pdb code 5w7f). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 6 binding sites of Calcium where determined in the
Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A, PDB code: 5w7f:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
6;
Calcium binding site 1 out
of 6 in 5w7f
Go back to
Calcium Binding Sites List in 5w7f
Calcium binding site 1 out
of 6 in the Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca601
b:64.4
occ:1.00
|
OD1
|
A:ASP187
|
2.3
|
62.2
|
1.0
|
|
OD2
|
A:ASP204
|
2.3
|
63.8
|
1.0
|
|
O
|
A:HIS189
|
2.4
|
68.2
|
1.0
|
|
OD1
|
A:ASP185
|
2.5
|
79.1
|
1.0
|
|
OD1
|
A:ASP207
|
2.5
|
58.0
|
1.0
|
|
OD2
|
A:ASP183
|
2.5
|
59.8
|
1.0
|
|
OD2
|
A:ASP185
|
2.9
|
77.8
|
1.0
|
|
CG
|
A:ASP187
|
3.0
|
70.2
|
1.0
|
|
CG
|
A:ASP185
|
3.0
|
76.4
|
1.0
|
|
HA
|
A:ASP207
|
3.0
|
95.4
|
1.0
|
|
OD2
|
A:ASP187
|
3.0
|
74.7
|
1.0
|
|
CG
|
A:ASP204
|
3.4
|
71.3
|
1.0
|
|
C
|
A:HIS189
|
3.6
|
50.2
|
1.0
|
|
HB2
|
A:ASP204
|
3.6
|
90.3
|
1.0
|
|
CG
|
A:ASP207
|
3.7
|
67.4
|
1.0
|
|
H
|
A:ASP187
|
3.7
|
69.8
|
1.0
|
|
HB3
|
A:ASP204
|
3.7
|
90.3
|
1.0
|
|
CG
|
A:ASP183
|
3.7
|
63.0
|
1.0
|
|
H
|
A:HIS189
|
3.7
|
76.2
|
1.0
|
|
CA
|
A:CA602
|
3.8
|
83.3
|
1.0
|
|
CB
|
A:ASP204
|
3.8
|
75.2
|
1.0
|
|
H
|
A:ASP185
|
3.9
|
75.7
|
1.0
|
|
CA
|
A:ASP207
|
3.9
|
79.5
|
1.0
|
|
HA
|
A:ASP183
|
3.9
|
65.5
|
1.0
|
|
HA
|
A:SER190
|
4.0
|
52.0
|
1.0
|
|
HB2
|
A:HIS189
|
4.0
|
69.0
|
1.0
|
|
O
|
A:ASP207
|
4.1
|
82.4
|
1.0
|
|
CB
|
A:ASP207
|
4.3
|
83.5
|
1.0
|
|
N
|
A:HIS189
|
4.3
|
63.5
|
1.0
|
|
CB
|
A:ASP187
|
4.4
|
66.0
|
1.0
|
|
OD1
|
A:ASP183
|
4.4
|
56.3
|
1.0
|
|
CA
|
A:HIS189
|
4.4
|
58.8
|
1.0
|
|
CB
|
A:ASP185
|
4.5
|
76.2
|
1.0
|
|
OD1
|
A:ASP204
|
4.5
|
77.5
|
1.0
|
|
N
|
A:ASP187
|
4.5
|
58.2
|
1.0
|
|
C
|
A:ASP207
|
4.5
|
87.2
|
1.0
|
|
H
|
A:SER186
|
4.5
|
78.4
|
1.0
|
|
HB2
|
A:ASP207
|
4.5
|
0.2
|
1.0
|
|
N
|
A:SER190
|
4.5
|
44.9
|
1.0
|
|
N
|
A:ASP185
|
4.7
|
63.1
|
1.0
|
|
OD2
|
A:ASP207
|
4.7
|
62.3
|
1.0
|
|
HB3
|
A:ASP187
|
4.7
|
79.2
|
1.0
|
|
CA
|
A:ASP183
|
4.7
|
54.5
|
1.0
|
|
CB
|
A:HIS189
|
4.7
|
57.5
|
1.0
|
|
H
|
A:VAL184
|
4.7
|
76.1
|
1.0
|
|
CA
|
A:SER190
|
4.7
|
43.4
|
1.0
|
|
CB
|
A:ASP183
|
4.7
|
56.1
|
1.0
|
|
O
|
A:ASN206
|
4.7
|
83.7
|
1.0
|
|
H
|
A:LYS188
|
4.8
|
83.2
|
1.0
|
|
HB3
|
A:ASP185
|
4.8
|
91.5
|
1.0
|
|
CA
|
A:ASP187
|
4.9
|
57.3
|
1.0
|
|
N
|
A:SER186
|
4.9
|
65.3
|
1.0
|
|
N
|
A:ASP207
|
5.0
|
76.8
|
1.0
|
|
HB2
|
A:ASP183
|
5.0
|
67.4
|
1.0
|
|
CA
|
A:ASP185
|
5.0
|
67.8
|
1.0
|
|
N
|
A:LYS188
|
5.0
|
69.3
|
1.0
|
|
Calcium binding site 2 out
of 6 in 5w7f
Go back to
Calcium Binding Sites List in 5w7f
Calcium binding site 2 out
of 6 in the Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca602
b:83.3
occ:1.00
|
OD2
|
A:ASP187
|
2.3
|
74.7
|
1.0
|
|
O
|
A:VAL212
|
2.3
|
70.4
|
1.0
|
|
O
|
A:ASP209
|
2.4
|
95.6
|
1.0
|
|
O
|
A:ASN206
|
2.4
|
83.7
|
1.0
|
|
OD2
|
A:ASP204
|
2.4
|
63.8
|
1.0
|
|
OD2
|
A:ASP185
|
2.5
|
77.8
|
1.0
|
|
OD1
|
A:ASP204
|
2.8
|
77.5
|
1.0
|
|
CG
|
A:ASP204
|
2.9
|
71.3
|
1.0
|
|
HB
|
A:VAL212
|
3.0
|
0.6
|
1.0
|
|
C
|
A:VAL212
|
3.4
|
82.6
|
1.0
|
|
H
|
A:VAL212
|
3.4
|
0.8
|
1.0
|
|
CG
|
A:ASP187
|
3.4
|
70.2
|
1.0
|
|
HA
|
A:ASP207
|
3.5
|
95.4
|
1.0
|
|
C
|
A:ASN206
|
3.5
|
82.6
|
1.0
|
|
C
|
A:ASP209
|
3.6
|
93.8
|
1.0
|
|
CG
|
A:ASP185
|
3.6
|
76.4
|
1.0
|
|
CB
|
A:VAL212
|
3.8
|
89.7
|
1.0
|
|
CA
|
A:CA601
|
3.8
|
64.4
|
1.0
|
|
HA
|
A:LYS210
|
3.8
|
96.1
|
1.0
|
|
CA
|
A:VAL212
|
3.9
|
92.0
|
1.0
|
|
HB3
|
A:ASN206
|
3.9
|
0.8
|
1.0
|
|
HG12
|
A:VAL212
|
3.9
|
0.9
|
1.0
|
|
N
|
A:VAL212
|
4.0
|
91.5
|
1.0
|
|
H
|
A:ASP209
|
4.0
|
98.2
|
1.0
|
|
HB3
|
A:ASP209
|
4.1
|
1.0
|
1.0
|
|
H
|
A:ASN206
|
4.1
|
0.8
|
1.0
|
|
CA
|
A:ASP207
|
4.2
|
79.5
|
1.0
|
|
OD1
|
A:ASP187
|
4.2
|
62.2
|
1.0
|
|
HB3
|
A:ASP187
|
4.2
|
79.2
|
1.0
|
|
OD1
|
A:ASP185
|
4.2
|
79.1
|
1.0
|
|
N
|
A:ASP207
|
4.2
|
76.8
|
1.0
|
|
HB3
|
A:TYR213
|
4.3
|
82.0
|
1.0
|
|
CG1
|
A:VAL212
|
4.4
|
93.3
|
1.0
|
|
CB
|
A:ASP187
|
4.4
|
66.0
|
1.0
|
|
CB
|
A:ASP204
|
4.4
|
75.2
|
1.0
|
|
N
|
A:ASP209
|
4.4
|
81.8
|
1.0
|
|
C
|
A:ASP207
|
4.5
|
87.2
|
1.0
|
|
CA
|
A:ASP209
|
4.5
|
88.9
|
1.0
|
|
N
|
A:LYS210
|
4.5
|
86.0
|
1.0
|
|
CA
|
A:ASN206
|
4.5
|
91.3
|
1.0
|
|
HA
|
A:TYR213
|
4.5
|
91.0
|
1.0
|
|
CA
|
A:LYS210
|
4.5
|
80.0
|
1.0
|
|
N
|
A:TYR213
|
4.5
|
82.8
|
1.0
|
|
HB2
|
A:ASP187
|
4.6
|
79.2
|
1.0
|
|
HG11
|
A:VAL212
|
4.7
|
0.9
|
1.0
|
|
N
|
A:ASN206
|
4.7
|
84.8
|
1.0
|
|
CB
|
A:ASN206
|
4.7
|
96.5
|
1.0
|
|
O
|
A:ASP207
|
4.7
|
82.4
|
1.0
|
|
HB2
|
A:ASP204
|
4.7
|
90.3
|
1.0
|
|
CB
|
A:ASP185
|
4.7
|
76.2
|
1.0
|
|
CB
|
A:ASP209
|
4.8
|
95.8
|
1.0
|
|
HB2
|
A:ASP185
|
4.8
|
91.5
|
1.0
|
|
HB3
|
A:ASP204
|
4.8
|
90.3
|
1.0
|
|
HB3
|
A:ASP185
|
4.8
|
91.5
|
1.0
|
|
C
|
A:LYS210
|
4.8
|
78.9
|
1.0
|
|
HA
|
A:VAL212
|
4.8
|
0.4
|
1.0
|
|
CA
|
A:TYR213
|
4.9
|
75.9
|
1.0
|
|
HG23
|
A:VAL212
|
4.9
|
0.9
|
1.0
|
|
CG2
|
A:VAL212
|
4.9
|
99.1
|
1.0
|
|
Calcium binding site 3 out
of 6 in 5w7f
Go back to
Calcium Binding Sites List in 5w7f
Calcium binding site 3 out
of 6 in the Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca603
b:78.9
occ:1.00
|
OD2
|
A:ASP222
|
2.3
|
96.6
|
1.0
|
|
OD2
|
A:ASP226
|
2.4
|
83.5
|
1.0
|
|
O
|
A:ILE232
|
2.4
|
0.8
|
1.0
|
|
OD1
|
A:ASN230
|
2.4
|
97.2
|
1.0
|
|
OE2
|
A:GLU244
|
2.5
|
91.5
|
1.0
|
|
OD1
|
A:ASN228
|
2.5
|
87.8
|
1.0
|
|
H
|
A:ILE232
|
3.3
|
0.7
|
1.0
|
|
CG
|
A:ASP226
|
3.4
|
92.2
|
1.0
|
|
HB
|
A:ILE232
|
3.5
|
0.4
|
1.0
|
|
CD
|
A:GLU244
|
3.5
|
98.7
|
1.0
|
|
CG
|
A:ASP222
|
3.5
|
0.4
|
1.0
|
|
CG
|
A:ASN230
|
3.5
|
83.7
|
1.0
|
|
H
|
A:ASN228
|
3.5
|
0.3
|
1.0
|
|
C
|
A:ILE232
|
3.6
|
0.7
|
1.0
|
|
CG
|
A:ASN228
|
3.6
|
84.1
|
1.0
|
|
HD21
|
A:ASN228
|
3.7
|
99.1
|
1.0
|
|
H
|
A:SER227
|
3.7
|
1.0
|
1.0
|
|
H
|
A:ASN230
|
3.8
|
89.8
|
1.0
|
|
HA
|
A:ASP226
|
3.8
|
0.6
|
1.0
|
|
OD1
|
A:ASP226
|
3.9
|
90.6
|
1.0
|
|
OE1
|
A:GLU244
|
4.0
|
83.4
|
1.0
|
|
N
|
A:ILE232
|
4.0
|
98.1
|
1.0
|
|
HD21
|
A:ASN230
|
4.1
|
96.2
|
1.0
|
|
ND2
|
A:ASN228
|
4.1
|
82.6
|
1.0
|
|
HB2
|
A:ASP222
|
4.1
|
0.3
|
1.0
|
|
CA
|
A:ILE232
|
4.1
|
0.1
|
1.0
|
|
ND2
|
A:ASN230
|
4.2
|
80.2
|
1.0
|
|
CB
|
A:ILE232
|
4.2
|
95.3
|
1.0
|
|
CB
|
A:ASP222
|
4.3
|
0.4
|
1.0
|
|
HB3
|
A:ASP222
|
4.3
|
0.3
|
1.0
|
|
HB3
|
A:TRP233
|
4.3
|
0.5
|
1.0
|
|
N
|
A:SER227
|
4.3
|
97.5
|
1.0
|
|
N
|
A:ASN228
|
4.4
|
92.8
|
1.0
|
|
HB2
|
A:GLU244
|
4.4
|
0.8
|
1.0
|
|
OD1
|
A:ASP222
|
4.5
|
0.7
|
1.0
|
|
N
|
A:ASN230
|
4.5
|
74.8
|
1.0
|
|
HG22
|
A:ILE232
|
4.5
|
0.8
|
1.0
|
|
CA
|
A:ASP226
|
4.5
|
0.3
|
1.0
|
|
CB
|
A:ASP226
|
4.5
|
97.1
|
1.0
|
|
HA
|
A:TRP233
|
4.6
|
0.9
|
1.0
|
|
CB
|
A:ASN230
|
4.6
|
68.5
|
1.0
|
|
HB3
|
A:ASN230
|
4.6
|
82.2
|
1.0
|
|
OG
|
A:SER227
|
4.6
|
95.6
|
1.0
|
|
CG
|
A:GLU244
|
4.7
|
0.8
|
1.0
|
|
N
|
A:TRP233
|
4.7
|
0.5
|
1.0
|
|
HG2
|
A:GLU244
|
4.7
|
0.5
|
1.0
|
|
H
|
A:GLY231
|
4.7
|
0.7
|
1.0
|
|
C
|
A:ASP226
|
4.9
|
93.9
|
1.0
|
|
H
|
A:CYS229
|
4.9
|
95.7
|
1.0
|
|
CB
|
A:ASN228
|
4.9
|
82.8
|
1.0
|
|
N
|
A:GLY231
|
4.9
|
84.0
|
1.0
|
|
CA
|
A:ASN230
|
4.9
|
75.3
|
1.0
|
|
HD22
|
A:ASN228
|
4.9
|
99.1
|
1.0
|
|
CG2
|
A:ILE232
|
4.9
|
0.8
|
1.0
|
|
C
|
A:ASN230
|
4.9
|
78.2
|
1.0
|
|
CA
|
A:TRP233
|
5.0
|
0.6
|
1.0
|
|
CA
|
A:ASN228
|
5.0
|
89.2
|
1.0
|
|
Calcium binding site 4 out
of 6 in 5w7f
Go back to
Calcium Binding Sites List in 5w7f
Calcium binding site 4 out
of 6 in the Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca601
b:64.7
occ:1.00
|
OD1
|
B:ASP207
|
2.3
|
65.4
|
1.0
|
|
OD2
|
B:ASP204
|
2.4
|
69.0
|
1.0
|
|
OD1
|
B:ASP183
|
2.4
|
61.5
|
1.0
|
|
O
|
B:HIS189
|
2.4
|
72.0
|
1.0
|
|
OD1
|
B:ASP187
|
2.6
|
47.0
|
1.0
|
|
OD1
|
B:ASP185
|
2.7
|
73.5
|
1.0
|
|
HA
|
B:ASP207
|
3.1
|
0.6
|
1.0
|
|
OD2
|
B:ASP185
|
3.2
|
60.5
|
1.0
|
|
CG
|
B:ASP185
|
3.2
|
63.4
|
1.0
|
|
CG
|
B:ASP187
|
3.3
|
58.6
|
1.0
|
|
CG
|
B:ASP204
|
3.4
|
74.6
|
1.0
|
|
OD2
|
B:ASP187
|
3.4
|
68.5
|
1.0
|
|
CG
|
B:ASP207
|
3.5
|
75.3
|
1.0
|
|
CG
|
B:ASP183
|
3.6
|
61.9
|
1.0
|
|
HB2
|
B:ASP204
|
3.6
|
92.9
|
1.0
|
|
C
|
B:HIS189
|
3.6
|
59.4
|
1.0
|
|
HB3
|
B:ASP204
|
3.7
|
92.9
|
1.0
|
|
HA
|
B:ASP183
|
3.7
|
78.1
|
1.0
|
|
CB
|
B:ASP204
|
3.8
|
77.4
|
1.0
|
|
H
|
B:HIS189
|
3.8
|
64.4
|
1.0
|
|
HA
|
B:SER190
|
3.8
|
68.2
|
1.0
|
|
H
|
B:ASP187
|
3.9
|
72.5
|
1.0
|
|
H
|
B:ASP185
|
3.9
|
80.5
|
1.0
|
|
CA
|
B:ASP207
|
4.0
|
84.6
|
1.0
|
|
CA
|
B:CA602
|
4.0
|
77.8
|
1.0
|
|
O
|
B:ASP207
|
4.1
|
79.4
|
1.0
|
|
HB2
|
B:HIS189
|
4.2
|
52.2
|
1.0
|
|
CB
|
B:ASP207
|
4.2
|
86.8
|
1.0
|
|
OD2
|
B:ASP183
|
4.3
|
58.5
|
1.0
|
|
N
|
B:HIS189
|
4.4
|
53.7
|
1.0
|
|
HB2
|
B:ASP207
|
4.4
|
0.2
|
1.0
|
|
OD2
|
B:ASP207
|
4.4
|
71.1
|
1.0
|
|
OD1
|
B:ASP204
|
4.5
|
81.0
|
1.0
|
|
CA
|
B:ASP183
|
4.5
|
65.1
|
1.0
|
|
CA
|
B:HIS189
|
4.5
|
51.3
|
1.0
|
|
N
|
B:SER190
|
4.5
|
53.4
|
1.0
|
|
H
|
B:VAL184
|
4.5
|
87.7
|
1.0
|
|
C
|
B:ASP207
|
4.5
|
83.1
|
1.0
|
|
CB
|
B:ASP183
|
4.5
|
61.2
|
1.0
|
|
H
|
B:SER186
|
4.6
|
85.4
|
1.0
|
|
CA
|
B:SER190
|
4.6
|
56.9
|
1.0
|
|
CB
|
B:ASP185
|
4.7
|
62.5
|
1.0
|
|
N
|
B:ASP185
|
4.7
|
67.1
|
1.0
|
|
N
|
B:ASP187
|
4.7
|
60.4
|
1.0
|
|
CB
|
B:ASP187
|
4.7
|
61.7
|
1.0
|
|
H
|
B:LYS188
|
4.8
|
72.8
|
1.0
|
|
CB
|
B:HIS189
|
4.8
|
43.5
|
1.0
|
|
HB2
|
B:ASP183
|
4.8
|
73.5
|
1.0
|
|
N
|
B:VAL184
|
4.8
|
73.1
|
1.0
|
|
C
|
B:ASP183
|
4.9
|
74.2
|
1.0
|
|
O
|
B:ASN206
|
4.9
|
87.7
|
1.0
|
|
HB3
|
B:ASP185
|
5.0
|
74.9
|
1.0
|
|
N
|
B:SER186
|
5.0
|
71.2
|
1.0
|
|
Calcium binding site 5 out
of 6 in 5w7f
Go back to
Calcium Binding Sites List in 5w7f
Calcium binding site 5 out
of 6 in the Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 5 of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca602
b:77.8
occ:1.00
|
O
|
B:VAL212
|
2.3
|
56.3
|
1.0
|
|
O
|
B:ASN206
|
2.3
|
87.7
|
1.0
|
|
O
|
B:ASP209
|
2.4
|
84.5
|
1.0
|
|
OD2
|
B:ASP187
|
2.4
|
68.5
|
1.0
|
|
OD2
|
B:ASP204
|
2.4
|
69.0
|
1.0
|
|
OD2
|
B:ASP185
|
2.6
|
60.5
|
1.0
|
|
OD1
|
B:ASP204
|
2.7
|
81.0
|
1.0
|
|
CG
|
B:ASP204
|
2.9
|
74.6
|
1.0
|
|
HB
|
B:VAL212
|
3.3
|
0.3
|
1.0
|
|
HA
|
B:ASP207
|
3.3
|
0.6
|
1.0
|
|
C
|
B:ASN206
|
3.4
|
92.6
|
1.0
|
|
C
|
B:VAL212
|
3.5
|
69.6
|
1.0
|
|
H
|
B:VAL212
|
3.5
|
92.0
|
1.0
|
|
C
|
B:ASP209
|
3.6
|
79.3
|
1.0
|
|
CG
|
B:ASP187
|
3.6
|
58.6
|
1.0
|
|
CG
|
B:ASP185
|
3.8
|
63.4
|
1.0
|
|
HA
|
B:LYS210
|
3.8
|
93.9
|
1.0
|
|
CA
|
B:CA601
|
4.0
|
64.7
|
1.0
|
|
HB3
|
B:ASN206
|
4.0
|
1.0
|
1.0
|
|
CB
|
B:VAL212
|
4.0
|
91.1
|
1.0
|
|
H
|
B:ASP209
|
4.0
|
99.8
|
1.0
|
|
H
|
B:ASN206
|
4.1
|
0.9
|
1.0
|
|
CA
|
B:ASP207
|
4.1
|
84.6
|
1.0
|
|
CA
|
B:VAL212
|
4.1
|
84.2
|
1.0
|
|
HB3
|
B:ASP209
|
4.1
|
0.5
|
1.0
|
|
HB3
|
B:TYR213
|
4.1
|
79.6
|
1.0
|
|
N
|
B:VAL212
|
4.1
|
76.7
|
1.0
|
|
HG12
|
B:VAL212
|
4.1
|
0.9
|
1.0
|
|
N
|
B:ASP207
|
4.2
|
88.5
|
1.0
|
|
OD1
|
B:ASP187
|
4.2
|
47.0
|
1.0
|
|
OD1
|
B:ASP185
|
4.3
|
73.5
|
1.0
|
|
C
|
B:ASP207
|
4.4
|
83.1
|
1.0
|
|
HA
|
B:TYR213
|
4.4
|
81.5
|
1.0
|
|
N
|
B:ASP209
|
4.4
|
83.1
|
1.0
|
|
CB
|
B:ASP204
|
4.4
|
77.4
|
1.0
|
|
CA
|
B:ASN206
|
4.5
|
95.6
|
1.0
|
|
N
|
B:LYS210
|
4.5
|
80.0
|
1.0
|
|
CA
|
B:LYS210
|
4.5
|
78.2
|
1.0
|
|
CA
|
B:ASP209
|
4.5
|
79.1
|
1.0
|
|
HB3
|
B:ASP187
|
4.5
|
74.0
|
1.0
|
|
O
|
B:ASP207
|
4.5
|
79.4
|
1.0
|
|
N
|
B:TYR213
|
4.6
|
61.1
|
1.0
|
|
CG1
|
B:VAL212
|
4.6
|
91.6
|
1.0
|
|
N
|
B:ASN206
|
4.6
|
85.8
|
1.0
|
|
CB
|
B:ASP187
|
4.7
|
61.7
|
1.0
|
|
CB
|
B:ASN206
|
4.7
|
0.3
|
1.0
|
|
HB2
|
B:ASP204
|
4.7
|
92.9
|
1.0
|
|
C
|
B:LYS210
|
4.7
|
73.1
|
1.0
|
|
CB
|
B:ASP209
|
4.8
|
86.2
|
1.0
|
|
CA
|
B:TYR213
|
4.8
|
67.9
|
1.0
|
|
HB3
|
B:ASP204
|
4.8
|
92.9
|
1.0
|
|
HB2
|
B:ASP187
|
4.9
|
74.0
|
1.0
|
|
CB
|
B:ASP185
|
4.9
|
62.5
|
1.0
|
|
HG11
|
B:VAL212
|
4.9
|
0.9
|
1.0
|
|
CB
|
B:TYR213
|
4.9
|
66.3
|
1.0
|
|
HB3
|
B:ASP185
|
5.0
|
74.9
|
1.0
|
|
HD2
|
B:TYR213
|
5.0
|
88.3
|
1.0
|
|
H
|
B:ASP207
|
5.0
|
0.2
|
1.0
|
|
Calcium binding site 6 out
of 6 in 5w7f
Go back to
Calcium Binding Sites List in 5w7f
Calcium binding site 6 out
of 6 in the Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 6 of Murine Acyloxyacyl Hydrolase (Aoah), S262A Mutant, with Lipid A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca603
b:89.3
occ:1.00
|
OE1
|
B:GLU244
|
2.3
|
84.3
|
1.0
|
|
OD2
|
B:ASP222
|
2.3
|
97.1
|
1.0
|
|
OD1
|
B:ASN228
|
2.3
|
87.8
|
1.0
|
|
OD1
|
B:ASN230
|
2.5
|
78.2
|
1.0
|
|
HD21
|
B:ASN228
|
3.0
|
78.6
|
1.0
|
|
CD
|
B:GLU244
|
3.0
|
85.0
|
1.0
|
|
OD2
|
B:ASP226
|
3.2
|
82.2
|
1.0
|
|
CG
|
B:ASN228
|
3.2
|
77.8
|
1.0
|
|
O
|
B:ILE232
|
3.2
|
98.2
|
1.0
|
|
CG
|
B:ASN230
|
3.3
|
75.6
|
1.0
|
|
OE2
|
B:GLU244
|
3.3
|
76.0
|
1.0
|
|
HB
|
B:ILE232
|
3.4
|
99.3
|
1.0
|
|
CG
|
B:ASP222
|
3.4
|
0.5
|
1.0
|
|
ND2
|
B:ASN228
|
3.4
|
65.5
|
1.0
|
|
HD21
|
B:ASN230
|
3.5
|
95.8
|
1.0
|
|
HG
|
B:SER227
|
3.5
|
0.8
|
1.0
|
|
H
|
B:ASN228
|
3.5
|
0.5
|
1.0
|
|
ND2
|
B:ASN230
|
3.7
|
79.9
|
1.0
|
|
H
|
B:SER227
|
3.9
|
0.4
|
1.0
|
|
H
|
B:ILE232
|
3.9
|
0.6
|
1.0
|
|
OD1
|
B:ASP222
|
4.0
|
0.7
|
1.0
|
|
HG2
|
B:GLU244
|
4.1
|
0.2
|
1.0
|
|
H
|
B:ASN230
|
4.1
|
83.3
|
1.0
|
|
CG
|
B:GLU244
|
4.2
|
0.7
|
1.0
|
|
OG
|
B:SER227
|
4.2
|
0.8
|
1.0
|
|
C
|
B:ILE232
|
4.2
|
96.4
|
1.0
|
|
CB
|
B:ILE232
|
4.3
|
82.7
|
1.0
|
|
HD22
|
B:ASN228
|
4.3
|
78.6
|
1.0
|
|
CG
|
B:ASP226
|
4.3
|
89.9
|
1.0
|
|
HB3
|
B:ASN230
|
4.4
|
80.3
|
1.0
|
|
HB2
|
B:GLU244
|
4.4
|
0.1
|
1.0
|
|
N
|
B:ASN228
|
4.4
|
90.4
|
1.0
|
|
CB
|
B:ASN230
|
4.4
|
66.9
|
1.0
|
|
HA
|
B:ASP226
|
4.4
|
0.9
|
1.0
|
|
HB3
|
B:PRO218
|
4.5
|
0.3
|
1.0
|
|
HD22
|
B:ASN230
|
4.5
|
95.8
|
1.0
|
|
HB2
|
B:ASP222
|
4.5
|
0.2
|
1.0
|
|
HG22
|
B:ILE232
|
4.5
|
0.3
|
1.0
|
|
N
|
B:SER227
|
4.6
|
98.7
|
1.0
|
|
N
|
B:ILE232
|
4.6
|
98.8
|
1.0
|
|
CA
|
B:ILE232
|
4.6
|
95.7
|
1.0
|
|
CB
|
B:ASN228
|
4.6
|
81.4
|
1.0
|
|
CB
|
B:ASP222
|
4.6
|
0.2
|
1.0
|
|
HA
|
B:PRO218
|
4.7
|
1.0
|
1.0
|
|
N
|
B:ASN230
|
4.8
|
69.4
|
1.0
|
|
OD1
|
B:ASP226
|
4.9
|
84.4
|
1.0
|
|
CB
|
B:GLU244
|
4.9
|
0.3
|
1.0
|
|
CG2
|
B:ILE232
|
4.9
|
84.4
|
1.0
|
|
HG3
|
B:GLU244
|
4.9
|
0.2
|
1.0
|
|
CA
|
B:ASN228
|
5.0
|
85.7
|
1.0
|
|
HB3
|
B:ASP222
|
5.0
|
0.2
|
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
|
