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Chlorine in PDB 3a0o: Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58

Protein crystallography data

The structure of Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58, PDB code: 3a0o was solved by A.Ochiai, M.Yamasaki, B.Mikami, W.Hashimoto, K.Murata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.85 / 2.11
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 64.153, 68.240, 108.895, 78.32, 89.29, 88.56
R / Rfree (%) 18.1 / 22.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58 (pdb code 3a0o). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58, PDB code: 3a0o:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3a0o

Go back to Chlorine Binding Sites List in 3a0o
Chlorine binding site 1 out of 2 in the Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1001

b:17.9
occ:1.00
N A:GLY358 3.3 15.9 1.0
CA A:GLY354 3.4 18.4 1.0
N A:ASP356 3.5 20.2 1.0
CB A:ASP356 3.5 20.5 1.0
CB A:PHE498 3.6 16.8 1.0
C A:GLY354 3.6 19.0 1.0
CA A:PHE498 3.7 17.1 1.0
CA A:GLY358 3.7 14.8 1.0
C A:PHE498 3.7 17.3 1.0
CA A:ASP356 3.8 19.9 1.0
N A:GLY357 3.9 18.5 1.0
N A:ASP499 3.9 17.8 1.0
N A:ASP500 3.9 17.6 1.0
C A:ASP356 3.9 19.2 1.0
N A:THR355 4.0 19.9 1.0
CB A:ASP500 4.0 17.3 1.0
O A:GLY354 4.1 18.6 1.0
O A:PHE498 4.2 17.0 1.0
CG1 A:ILE501 4.2 14.4 1.0
N A:ILE501 4.2 15.9 1.0
CD2 A:PHE498 4.3 16.7 1.0
N A:GLY354 4.3 17.8 1.0
CG A:ASP356 4.3 21.7 1.0
OD2 A:ASP356 4.4 24.1 1.0
CA A:ASP500 4.4 17.1 1.0
CG A:PHE498 4.4 16.4 1.0
C A:GLY357 4.5 16.6 1.0
CG2 A:ILE501 4.5 14.2 1.0
C A:THR355 4.6 20.5 1.0
C A:GLY358 4.6 14.2 1.0
O A:ASP356 4.6 19.2 1.0
O A:GLY358 4.7 14.2 1.0
C A:ASP499 4.7 18.1 1.0
CG A:ASP500 4.8 17.9 1.0
CA A:GLY357 4.8 17.3 1.0
C A:ASP500 4.8 16.6 1.0
CB A:ILE501 4.8 15.0 1.0
CA A:THR355 4.9 20.8 1.0
CA A:ASP499 4.9 18.6 1.0
CD1 A:ILE501 4.9 14.7 1.0

Chlorine binding site 2 out of 2 in 3a0o

Go back to Chlorine Binding Sites List in 3a0o
Chlorine binding site 2 out of 2 in the Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Alginate Lyase From Agrobacterium Tumefaciens C58 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1001

b:20.1
occ:1.00
O B:HOH2442 3.2 35.0 1.0
N B:GLY358 3.4 16.1 1.0
N B:ASP356 3.5 22.1 1.0
CA B:GLY354 3.5 20.9 1.0
CB B:PHE498 3.5 17.3 1.0
CB B:ASP356 3.5 21.9 1.0
CA B:PHE498 3.6 17.5 1.0
C B:PHE498 3.7 17.9 1.0
C B:GLY354 3.7 21.6 1.0
CA B:GLY358 3.7 15.2 1.0
CA B:ASP356 3.8 21.4 1.0
N B:GLY357 3.9 19.1 1.0
N B:ASP500 4.0 18.8 1.0
N B:ASP499 4.0 18.5 1.0
C B:ASP356 4.0 20.3 1.0
N B:THR355 4.0 22.3 1.0
CB B:ASP500 4.0 18.6 1.0
O B:PHE498 4.1 17.4 1.0
O B:GLY354 4.1 21.5 1.0
CG1 B:ILE501 4.1 15.4 1.0
CD2 B:PHE498 4.1 16.1 1.0
N B:ILE501 4.2 16.7 1.0
CG B:PHE498 4.3 16.8 1.0
N B:GLY354 4.4 19.9 1.0
CG B:ASP356 4.4 23.7 1.0
CA B:ASP500 4.5 18.4 1.0
CG2 B:ILE501 4.5 15.2 1.0
C B:GLY357 4.5 16.7 1.0
OD2 B:ASP356 4.5 24.9 1.0
C B:THR355 4.6 22.7 1.0
C B:GLY358 4.6 14.7 1.0
O B:GLY358 4.7 14.3 1.0
O B:ASP356 4.7 20.1 1.0
CD1 B:ILE501 4.8 15.6 1.0
CB B:ILE501 4.8 15.6 1.0
CG B:ASP500 4.8 19.8 1.0
CA B:GLY357 4.8 17.6 1.0
C B:ASP499 4.8 19.2 1.0
C B:ASP500 4.8 17.9 1.0
CA B:THR355 4.9 23.0 1.0
CA B:ASP499 5.0 19.3 1.0

Reference:

A.Ochiai, M.Yamasaki, B.Mikami, W.Hashimoto, K.Murata. Crystal Structure of Exotype Alginate Lyase ATU3025 From Agrobacterium Tumefaciens J.Biol.Chem. V. 285 24519 2010.
ISSN: ISSN 0021-9258
PubMed: 20507980
DOI: 10.1074/JBC.M110.125450
Page generated: Sat Dec 12 09:30:54 2020

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