Zinc in PDB 4ok4: Crystal Structure of ALG17C Mutant H202L
Protein crystallography data
The structure of Crystal Structure of ALG17C Mutant H202L, PDB code: 4ok4
was solved by
S.K.Nair,
D.S.Park,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.00 /
1.70
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
86.470,
127.153,
88.277,
90.00,
111.20,
90.00
|
R / Rfree (%)
|
19.3 /
21.7
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of ALG17C Mutant H202L
(pdb code 4ok4). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Crystal Structure of ALG17C Mutant H202L, PDB code: 4ok4:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 4ok4
Go back to
Zinc Binding Sites List in 4ok4
Zinc binding site 1 out
of 2 in the Crystal Structure of ALG17C Mutant H202L
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of ALG17C Mutant H202L within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn800
b:11.7
occ:1.00
|
NE2
|
A:HIS464
|
2.1
|
7.6
|
1.0
|
O
|
A:HOH1590
|
2.1
|
8.0
|
1.0
|
O
|
A:HOH1238
|
2.2
|
7.9
|
1.0
|
O
|
A:HOH914
|
2.2
|
10.0
|
1.0
|
ND1
|
A:HIS415
|
2.2
|
10.9
|
1.0
|
OD1
|
A:ASP433
|
2.3
|
8.6
|
1.0
|
CE1
|
A:HIS415
|
3.0
|
11.0
|
1.0
|
CD2
|
A:HIS464
|
3.0
|
7.7
|
1.0
|
CE1
|
A:HIS464
|
3.1
|
7.8
|
1.0
|
CG
|
A:ASP433
|
3.2
|
8.6
|
1.0
|
CG
|
A:HIS415
|
3.3
|
10.9
|
1.0
|
OD2
|
A:ASP433
|
3.4
|
8.7
|
1.0
|
CB
|
A:HIS415
|
3.8
|
11.0
|
1.0
|
O
|
A:HOH924
|
3.9
|
10.3
|
1.0
|
O
|
A:ALA458
|
4.0
|
8.5
|
1.0
|
N
|
A:ASN310
|
4.1
|
10.4
|
1.0
|
NE2
|
A:HIS415
|
4.2
|
10.9
|
1.0
|
OD2
|
A:ASP417
|
4.2
|
12.2
|
1.0
|
CG
|
A:HIS464
|
4.2
|
7.7
|
1.0
|
ND1
|
A:HIS464
|
4.2
|
7.8
|
1.0
|
O
|
A:ASN310
|
4.2
|
10.6
|
1.0
|
N
|
A:GLY435
|
4.3
|
8.9
|
1.0
|
CD2
|
A:HIS415
|
4.3
|
10.9
|
1.0
|
O
|
A:GLY435
|
4.4
|
9.4
|
1.0
|
O
|
A:PRO308
|
4.5
|
10.7
|
1.0
|
CA
|
A:ASN310
|
4.5
|
10.4
|
1.0
|
CB
|
A:ASP433
|
4.6
|
8.6
|
1.0
|
CA
|
A:GLY435
|
4.7
|
9.3
|
1.0
|
N
|
A:TYR434
|
4.7
|
8.7
|
1.0
|
C
|
A:ASN310
|
4.7
|
10.6
|
1.0
|
CA
|
A:ILE309
|
4.9
|
10.6
|
1.0
|
C
|
A:ILE309
|
4.9
|
10.4
|
1.0
|
C
|
A:GLY435
|
4.9
|
9.4
|
1.0
|
CG
|
A:ASP417
|
4.9
|
11.8
|
1.0
|
|
Zinc binding site 2 out
of 2 in 4ok4
Go back to
Zinc Binding Sites List in 4ok4
Zinc binding site 2 out
of 2 in the Crystal Structure of ALG17C Mutant H202L
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of ALG17C Mutant H202L within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn800
b:8.4
occ:1.00
|
NE2
|
B:HIS464
|
2.1
|
5.1
|
1.0
|
O
|
B:HOH914
|
2.1
|
4.0
|
1.0
|
O
|
B:HOH903
|
2.2
|
4.4
|
1.0
|
ND1
|
B:HIS415
|
2.2
|
6.7
|
1.0
|
O
|
B:HOH910
|
2.3
|
7.1
|
1.0
|
OD1
|
B:ASP433
|
2.3
|
6.2
|
1.0
|
CE1
|
B:HIS415
|
3.0
|
6.7
|
1.0
|
CD2
|
B:HIS464
|
3.0
|
5.2
|
1.0
|
CE1
|
B:HIS464
|
3.2
|
5.2
|
1.0
|
CG
|
B:ASP433
|
3.2
|
6.3
|
1.0
|
CG
|
B:HIS415
|
3.3
|
6.8
|
1.0
|
OD2
|
B:ASP433
|
3.4
|
6.2
|
1.0
|
CB
|
B:HIS415
|
3.8
|
7.1
|
1.0
|
O
|
B:HOH918
|
3.9
|
6.4
|
1.0
|
O
|
B:ALA458
|
4.0
|
6.2
|
1.0
|
N
|
B:ASN310
|
4.1
|
7.1
|
1.0
|
NE2
|
B:HIS415
|
4.2
|
6.6
|
1.0
|
CG
|
B:HIS464
|
4.2
|
5.2
|
1.0
|
ND1
|
B:HIS464
|
4.2
|
5.2
|
1.0
|
OD2
|
B:ASP417
|
4.3
|
9.7
|
1.0
|
O
|
B:ASN310
|
4.3
|
7.1
|
1.0
|
N
|
B:GLY435
|
4.3
|
6.1
|
1.0
|
O
|
B:GLY435
|
4.3
|
6.3
|
1.0
|
CD2
|
B:HIS415
|
4.4
|
6.7
|
1.0
|
O
|
B:PRO308
|
4.5
|
7.6
|
1.0
|
CA
|
B:ASN310
|
4.6
|
7.2
|
1.0
|
CB
|
B:ASP433
|
4.6
|
6.2
|
1.0
|
N
|
B:TYR434
|
4.7
|
6.1
|
1.0
|
CA
|
B:GLY435
|
4.7
|
6.2
|
1.0
|
C
|
B:ASN310
|
4.8
|
7.1
|
1.0
|
C
|
B:ILE309
|
4.9
|
7.3
|
1.0
|
CA
|
B:ILE309
|
4.9
|
7.3
|
1.0
|
C
|
B:GLY435
|
4.9
|
6.3
|
1.0
|
CG
|
B:ASP417
|
4.9
|
9.4
|
1.0
|
|
Reference:
D.Park,
S.Jagtap,
S.K.Nair.
Structure of A PL17 Family Alginate Lyase Demonstrates Functional Similarities Among Exotype Depolymerases. J.Biol.Chem. V. 289 8645 2014.
ISSN: ISSN 0021-9258
PubMed: 24478312
DOI: 10.1074/JBC.M113.531111
Page generated: Sun Oct 27 03:49:44 2024
|