Calcium in PDB 1y3g: Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin
Enzymatic activity of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin
All present enzymatic activity of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin:
3.4.24.27;
Protein crystallography data
The structure of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin, PDB code: 1y3g
was solved by
D.H.Juers,
J.Kim,
B.W.Matthews,
S.M.Sieburth,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
31.00 /
2.10
|
Space group
|
P 61 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.520,
93.520,
131.770,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
15.5 /
22.5
|
Other elements in 1y3g:
The structure of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin
(pdb code 1y3g). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the
Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin, PDB code: 1y3g:
Jump to Calcium binding site number:
1;
2;
3;
4;
Calcium binding site 1 out
of 4 in 1y3g
Go back to
Calcium Binding Sites List in 1y3g
Calcium binding site 1 out
of 4 in the Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca317
b:15.9
occ:1.00
|
O
|
E:GLU187
|
2.3
|
10.8
|
1.0
|
OE1
|
E:GLU177
|
2.4
|
19.3
|
1.0
|
OD2
|
E:ASP138
|
2.4
|
12.2
|
1.0
|
OD1
|
E:ASP185
|
2.4
|
16.1
|
1.0
|
OE2
|
E:GLU190
|
2.5
|
13.4
|
1.0
|
O
|
E:HOH346
|
2.6
|
10.4
|
1.0
|
OE1
|
E:GLU190
|
2.6
|
14.3
|
1.0
|
OE2
|
E:GLU177
|
2.7
|
19.7
|
1.0
|
CD
|
E:GLU177
|
2.8
|
16.1
|
1.0
|
CD
|
E:GLU190
|
2.9
|
19.0
|
1.0
|
CG
|
E:ASP185
|
3.3
|
18.1
|
1.0
|
C
|
E:GLU187
|
3.4
|
14.8
|
1.0
|
CG
|
E:ASP138
|
3.5
|
14.0
|
1.0
|
OD2
|
E:ASP185
|
3.6
|
17.1
|
1.0
|
CA
|
E:CA318
|
3.7
|
19.6
|
1.0
|
CB
|
E:ASP138
|
4.0
|
9.8
|
1.0
|
O
|
E:ASP185
|
4.1
|
21.7
|
1.0
|
N
|
E:GLU187
|
4.2
|
20.2
|
1.0
|
CA
|
E:GLU187
|
4.2
|
18.9
|
1.0
|
N
|
E:ILE188
|
4.2
|
14.9
|
1.0
|
OD1
|
E:ASP138
|
4.3
|
19.7
|
1.0
|
CG
|
E:GLU177
|
4.3
|
14.4
|
1.0
|
CG
|
E:GLU190
|
4.3
|
16.7
|
1.0
|
CA
|
E:ILE188
|
4.3
|
19.6
|
1.0
|
N
|
E:GLY189
|
4.4
|
18.9
|
1.0
|
C
|
E:ASP185
|
4.6
|
24.2
|
1.0
|
CB
|
E:GLU187
|
4.6
|
21.4
|
1.0
|
O
|
E:HOH350
|
4.7
|
22.6
|
1.0
|
CB
|
E:ASP185
|
4.7
|
17.3
|
1.0
|
N
|
E:ASP185
|
4.7
|
21.2
|
1.0
|
C
|
E:ILE188
|
4.8
|
25.0
|
1.0
|
CB
|
E:GLU177
|
4.9
|
14.8
|
1.0
|
O
|
E:HOH353
|
4.9
|
21.5
|
1.0
|
CA
|
E:ASP185
|
4.9
|
14.5
|
1.0
|
N
|
E:GLU190
|
5.0
|
14.5
|
1.0
|
|
Calcium binding site 2 out
of 4 in 1y3g
Go back to
Calcium Binding Sites List in 1y3g
Calcium binding site 2 out
of 4 in the Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca318
b:19.6
occ:1.00
|
OE2
|
E:GLU190
|
2.2
|
13.4
|
1.0
|
OD2
|
E:ASP185
|
2.3
|
17.1
|
1.0
|
O
|
E:HOH475
|
2.4
|
22.2
|
1.0
|
OE2
|
E:GLU177
|
2.4
|
19.7
|
1.0
|
O
|
E:HOH353
|
2.4
|
21.5
|
1.0
|
O
|
E:ASN183
|
2.4
|
21.6
|
1.0
|
CG
|
E:ASP185
|
3.3
|
18.1
|
1.0
|
CD
|
E:GLU177
|
3.3
|
16.1
|
1.0
|
CD
|
E:GLU190
|
3.4
|
19.0
|
1.0
|
C
|
E:ASN183
|
3.6
|
16.6
|
1.0
|
CA
|
E:CA317
|
3.7
|
15.9
|
1.0
|
OD1
|
E:ASP185
|
3.7
|
16.1
|
1.0
|
OE1
|
E:GLU177
|
3.8
|
19.3
|
1.0
|
CG
|
E:GLU190
|
3.8
|
16.7
|
1.0
|
O
|
E:LYS182
|
3.8
|
37.4
|
1.0
|
N
|
E:ASP185
|
4.1
|
21.2
|
1.0
|
CG
|
E:GLU177
|
4.2
|
14.4
|
1.0
|
C
|
E:PRO184
|
4.2
|
27.6
|
1.0
|
CA
|
E:PRO184
|
4.3
|
21.7
|
1.0
|
OD1
|
E:ASP191
|
4.3
|
25.1
|
1.0
|
CB
|
E:ASN183
|
4.3
|
26.2
|
1.0
|
CB
|
E:ASP185
|
4.3
|
17.3
|
1.0
|
OD2
|
E:ASP191
|
4.3
|
19.6
|
1.0
|
OE1
|
E:GLU190
|
4.3
|
14.3
|
1.0
|
N
|
E:PRO184
|
4.3
|
22.3
|
1.0
|
CA
|
E:ASN183
|
4.5
|
16.5
|
1.0
|
CG
|
E:ASP191
|
4.6
|
21.0
|
1.0
|
CA
|
E:ASP185
|
4.8
|
14.5
|
1.0
|
O
|
E:PRO184
|
4.9
|
22.5
|
1.0
|
C
|
E:LYS182
|
4.9
|
41.5
|
1.0
|
|
Calcium binding site 3 out
of 4 in 1y3g
Go back to
Calcium Binding Sites List in 1y3g
Calcium binding site 3 out
of 4 in the Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca319
b:17.0
occ:1.00
|
O
|
E:GLN61
|
2.1
|
18.5
|
1.0
|
O
|
E:HOH503
|
2.2
|
16.1
|
1.0
|
OD1
|
E:ASP59
|
2.4
|
19.8
|
1.0
|
O
|
E:HOH419
|
2.4
|
13.6
|
1.0
|
O
|
E:HOH482
|
2.4
|
25.1
|
1.0
|
OD1
|
E:ASP57
|
2.4
|
19.7
|
1.0
|
OD2
|
E:ASP57
|
2.6
|
14.1
|
1.0
|
CG
|
E:ASP57
|
2.8
|
18.6
|
1.0
|
C
|
E:GLN61
|
3.3
|
25.9
|
1.0
|
CG
|
E:ASP59
|
3.3
|
20.2
|
1.0
|
OD2
|
E:ASP59
|
3.8
|
24.5
|
1.0
|
O
|
E:HOH484
|
3.8
|
33.3
|
1.0
|
N
|
E:GLN61
|
3.9
|
24.5
|
1.0
|
CA
|
E:GLN61
|
4.0
|
22.2
|
1.0
|
CB
|
E:ASP57
|
4.3
|
20.1
|
1.0
|
CB
|
E:GLN61
|
4.3
|
18.7
|
1.0
|
N
|
E:ASP59
|
4.4
|
15.8
|
1.0
|
N
|
E:PHE62
|
4.4
|
17.0
|
1.0
|
O
|
E:HOH508
|
4.5
|
24.9
|
1.0
|
OD2
|
E:ASP67
|
4.6
|
19.7
|
1.0
|
CA
|
E:PHE62
|
4.6
|
16.9
|
1.0
|
CB
|
E:ASP59
|
4.6
|
17.6
|
1.0
|
N
|
E:ASN60
|
4.7
|
23.4
|
1.0
|
O
|
E:HOH356
|
4.7
|
22.8
|
1.0
|
N
|
E:ALA58
|
4.8
|
14.1
|
1.0
|
CA
|
E:ASP59
|
4.8
|
17.9
|
1.0
|
C
|
E:ASP59
|
5.0
|
12.6
|
1.0
|
|
Calcium binding site 4 out
of 4 in 1y3g
Go back to
Calcium Binding Sites List in 1y3g
Calcium binding site 4 out
of 4 in the Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of Crystal Structure of A Silanediol Protease Inhibitor Bound to Thermolysin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca320
b:22.5
occ:1.00
|
OG1
|
E:THR194
|
2.1
|
20.9
|
1.0
|
O
|
E:HOH480
|
2.1
|
27.4
|
1.0
|
OD1
|
E:ASP200
|
2.2
|
18.3
|
1.0
|
O
|
E:ILE197
|
2.2
|
44.9
|
1.0
|
O
|
E:TYR193
|
2.3
|
19.5
|
1.0
|
O
|
E:THR194
|
2.3
|
19.8
|
1.0
|
O
|
E:HOH354
|
2.5
|
17.1
|
1.0
|
C
|
E:THR194
|
3.1
|
24.9
|
1.0
|
CG
|
E:ASP200
|
3.2
|
20.4
|
1.0
|
C
|
E:TYR193
|
3.2
|
16.3
|
1.0
|
CB
|
E:THR194
|
3.2
|
19.3
|
1.0
|
C
|
E:ILE197
|
3.3
|
40.5
|
1.0
|
CA
|
E:THR194
|
3.5
|
15.2
|
1.0
|
OD2
|
E:ASP200
|
3.5
|
16.1
|
1.0
|
N
|
E:ILE197
|
3.6
|
53.0
|
1.0
|
N
|
E:THR194
|
3.7
|
18.1
|
1.0
|
CA
|
E:ILE197
|
3.9
|
31.9
|
1.0
|
N
|
E:PRO195
|
4.2
|
23.0
|
1.0
|
CB
|
E:ILE197
|
4.2
|
31.6
|
1.0
|
N
|
E:SER198
|
4.4
|
38.4
|
1.0
|
O
|
E:ASP200
|
4.4
|
24.6
|
1.0
|
CA
|
E:TYR193
|
4.5
|
15.1
|
1.0
|
CG2
|
E:THR194
|
4.5
|
16.6
|
1.0
|
CB
|
E:ASP200
|
4.5
|
17.2
|
1.0
|
O
|
E:HOH476
|
4.5
|
34.7
|
1.0
|
O
|
E:GLU190
|
4.6
|
24.8
|
1.0
|
CA
|
E:SER198
|
4.6
|
42.2
|
1.0
|
CB
|
E:TYR193
|
4.6
|
16.6
|
1.0
|
CD2
|
E:TYR193
|
4.7
|
23.6
|
1.0
|
N
|
E:ASP200
|
4.7
|
25.3
|
1.0
|
C
|
E:ASP200
|
4.7
|
28.1
|
1.0
|
C
|
E:GLY196
|
4.8
|
59.2
|
1.0
|
CG2
|
E:ILE197
|
4.8
|
23.2
|
1.0
|
CA
|
E:ASP200
|
4.8
|
16.5
|
1.0
|
CA
|
E:PRO195
|
4.9
|
33.9
|
1.0
|
CG
|
E:TYR193
|
5.0
|
22.2
|
1.0
|
CA
|
E:GLY196
|
5.0
|
43.0
|
1.0
|
|
Reference:
D.H.Juers,
J.Kim,
B.W.Matthews,
S.M.Sieburth.
Structural Analysis of Silanediols As Transition-State-Analogue Inhibitors of the Benchmark Metalloprotease Thermolysin(,). Biochemistry V. 44 16524 2005.
ISSN: ISSN 0006-2960
PubMed: 16342943
DOI: 10.1021/BI051346V
Page generated: Fri Jul 12 07:57:35 2024
|