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Zinc in PDB 5ezm: Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State

Enzymatic activity of Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State

All present enzymatic activity of Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State:
2.4.2.43;

Protein crystallography data

The structure of Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State, PDB code: 5ezm was solved by V.I.Petrou, O.B.Clarke, D.Tomasek, S.Banerjee, K.R.Rajashankar, F.Mancia, New York Consortium On Membrane Protein Structure (Nycomps), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.41 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.604, 80.630, 150.253, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 26

Other elements in 5ezm:

The structure of Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State (pdb code 5ezm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State, PDB code: 5ezm:

Zinc binding site 1 out of 1 in 5ezm

Go back to Zinc Binding Sites List in 5ezm
Zinc binding site 1 out of 1 in the Crystal Structure of Arnt From Cupriavidus Metallidurans in the Apo State


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 Arnt From Cupriavidus Metallidurans in the Apo State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:31.2
occ:0.41
 ND1 A:HIS267 2.0 79.2 1.0
NE2 A:HIS265 2.0 79.2 1.0
OE2 A:GLU84 2.0 76.2 1.0
OE1 A:GLU84 2.1 76.8 1.0
CD A:GLU84 2.4 75.2 1.0
CD2 A:HIS265 2.8 78.4 1.0
CG A:HIS267 2.9 79.5 1.0
CE1 A:HIS267 2.9 78.4 1.0
CE1 A:HIS265 3.1 80.2 1.0
CB A:HIS267 3.2 80.9 1.0
CA A:HIS267 3.7 83.7 1.0
CG A:GLU84 3.9 71.6 1.0
CD2 A:HIS267 3.9 78.5 1.0
NE2 A:HIS267 3.9 77.5 1.0
CG A:HIS265 4.0 80.1 1.0
ND1 A:HIS265 4.1 81.6 1.0
CZ A:PHE261 4.3 55.7 1.0
O A:HOH727 4.3 60.9 1.0
O A:HOH708 4.4 70.3 1.0
N A:HIS267 4.7 82.6 1.0
N A:TRP268 4.7 94.1 1.0
C A:HIS267 4.8 88.4 1.0
CB A:GLU84 4.8 68.0 1.0

Reference:

V.I.Petrou, C.M.Herrera, K.M.Schultz, O.B.Clarke, J.Vendome, D.Tomasek, S.Banerjee, K.R.Rajashankar, M.Belcher Dufrisne, B.Kloss, E.Kloppmann, B.Rost, C.S.Klug, M.S.Trent, L.Shapiro, F.Mancia. Structures of Aminoarabinose Transferase Arnt Suggest A Molecular Basis For Lipid A Glycosylation. Science V. 351 608 2016.
ISSN: ESSN 1095-9203
PubMed: 26912703
DOI: 10.1126/SCIENCE.AAD1172
Page generated: Sun Oct 27 15:37:20 2024

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