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Zinc in PDB 3cxk: 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card.

Protein crystallography data

The structure of 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card., PDB code: 3cxk was solved by S.Lovell, C.Gerdts, B.Staker, D.Craigen, L.Stewart, Acceleratedtechnologies Center For Gene To 3D Structure (Atcg3D), Seattlestructural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.70
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 41.997, 45.171, 45.402, 88.41, 83.73, 69.10
R / Rfree (%) 16.6 / 19.9

Zinc Binding Sites:

The binding sites of Zinc atom in the 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card. (pdb code 3cxk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card., PDB code: 3cxk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3cxk

Go back to Zinc Binding Sites List in 3cxk
Zinc binding site 1 out of 2 in the 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:22.6
occ:1.00
SG A:CYS58 2.3 24.0 1.0
SG A:CYS107 2.3 22.4 1.0
SG A:CYS55 2.3 22.3 1.0
SG A:CYS104 2.4 24.5 1.0
CB A:CYS104 3.1 22.0 1.0
CB A:CYS55 3.2 18.9 1.0
CB A:CYS107 3.3 23.8 1.0
CB A:CYS58 3.3 24.4 1.0
N A:CYS58 3.8 23.5 1.0
N A:CYS107 3.9 24.2 1.0
CA A:CYS58 4.1 23.3 1.0
CA A:CYS107 4.2 23.6 1.0
CB A:VAL57 4.4 23.3 1.0
CB A:ALA109 4.5 20.4 1.0
CB A:GLN106 4.5 27.9 1.0
CA A:CYS104 4.6 21.8 1.0
CA A:CYS55 4.6 20.1 1.0
C A:GLN106 4.8 26.4 1.0
CG1 A:VAL57 4.8 25.1 1.0
C A:VAL57 4.8 24.4 1.0
C A:CYS107 4.8 23.4 1.0
OG1 A:THR60 4.9 25.8 1.0
C A:CYS58 4.9 24.2 1.0
N A:GLY108 4.9 21.5 1.0
CB A:THR60 4.9 23.4 1.0
N A:GLY59 4.9 23.2 1.0
N A:ALA109 4.9 19.7 1.0
CA A:VAL57 5.0 22.7 1.0
N A:VAL57 5.0 21.6 1.0

Zinc binding site 2 out of 2 in 3cxk

Go back to Zinc Binding Sites List in 3cxk
Zinc binding site 2 out of 2 in the 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of 1.7 A Crystal Structure of Methionine-R-Sulfoxide Reductase From Burkholderia Pseudomallei: Crystallization in A Microfluidic Crystal Card. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:23.0
occ:1.00
SG B:CYS58 2.3 24.8 1.0
SG B:CYS55 2.3 21.6 1.0
SG B:CYS104 2.3 23.4 1.0
SG B:CYS107 2.4 24.2 1.0
CB B:CYS104 3.2 22.1 1.0
CB B:CYS55 3.2 19.0 1.0
CB B:CYS107 3.4 23.8 1.0
CB B:CYS58 3.4 23.8 1.0
N B:CYS107 3.8 25.6 1.0
N B:CYS58 3.8 24.4 1.0
CA B:CYS107 4.1 23.9 1.0
CA B:CYS58 4.2 24.2 1.0
CB B:ALA109 4.4 22.6 1.0
CB B:VAL57 4.5 24.0 1.0
CA B:CYS104 4.6 21.9 1.0
CA B:CYS55 4.6 18.9 1.0
CB B:GLN106 4.7 30.1 1.0
C B:GLN106 4.7 28.1 1.0
C B:CYS107 4.8 24.4 1.0
C B:VAL57 4.8 24.6 1.0
OG1 B:THR60 4.8 26.0 1.0
N B:ALA109 4.9 22.8 1.0
N B:GLY108 4.9 22.4 1.0
C B:CYS58 4.9 25.2 1.0
CB B:THR60 4.9 24.8 1.0
N B:GLY59 5.0 24.0 1.0

Reference:

C.J.Gerdts, M.Elliott, S.Lovell, M.B.Mixon, A.J.Napuli, B.L.Staker, P.Nollert, L.Stewart. The Plug-Based Nanovolume Microcapillary Protein Crystallization System (Mpcs). Acta Crystallogr.,Sect.D V. 64 1116 2008.
ISSN: ISSN 0907-4449
PubMed: 19020349
DOI: 10.1107/S0907444908028060
Page generated: Thu Oct 24 11:58:16 2024

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