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Zinc in PDB 4axv: Biochemical and Structural Characterization of the Mpaa Amidase As Part of A Conserved Scavenging Pathway For Peptidoglycan Derived Peptides in Gamma-Proteobacteria

Protein crystallography data

The structure of Biochemical and Structural Characterization of the Mpaa Amidase As Part of A Conserved Scavenging Pathway For Peptidoglycan Derived Peptides in Gamma-Proteobacteria, PDB code: 4axv was solved by A.Maqbool, M.Herve, D.Mengin-Lecreulx, E.Dodson, A.J.Wilkinson, G.H.Thomas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.96 / 2.17
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.600, 73.600, 208.710, 90.00, 90.00, 120.00
R / Rfree (%) 19.572 / 23.293

Zinc Binding Sites:

The binding sites of Zinc atom in the Biochemical and Structural Characterization of the Mpaa Amidase As Part of A Conserved Scavenging Pathway For Peptidoglycan Derived Peptides in Gamma-Proteobacteria (pdb code 4axv). 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 Biochemical and Structural Characterization of the Mpaa Amidase As Part of A Conserved Scavenging Pathway For Peptidoglycan Derived Peptides in Gamma-Proteobacteria, PDB code: 4axv:

Zinc binding site 1 out of 1 in 4axv

Go back to Zinc Binding Sites List in 4axv
Zinc binding site 1 out of 1 in the Biochemical and Structural Characterization of the Mpaa Amidase As Part of A Conserved Scavenging Pathway For Peptidoglycan Derived Peptides in Gamma-Proteobacteria


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Biochemical and Structural Characterization of the Mpaa Amidase As Part of A Conserved Scavenging Pathway For Peptidoglycan Derived Peptides in Gamma-Proteobacteria within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:54.4
occ:1.00
OE1 A:GLU51 2.1 28.8 1.0
OE2 A:GLU51 2.2 31.1 1.0
ND1 A:HIS156 2.2 36.9 1.0
ND1 A:HIS48 2.2 31.6 1.0
O A:HOH2017 2.4 47.5 1.0
CD A:GLU51 2.5 28.6 1.0
CE1 A:HIS48 3.0 29.2 1.0
CE1 A:HIS156 3.1 33.1 1.0
CG A:HIS156 3.2 29.3 1.0
CG A:HIS48 3.3 25.7 1.0
CB A:HIS156 3.6 26.4 1.0
CB A:HIS48 3.7 25.2 1.0
O A:GLU157 3.8 27.9 1.0
O A:HOH2014 3.9 26.1 1.0
CG A:GLU51 4.0 26.0 1.0
NE2 A:HIS48 4.2 30.1 1.0
NE2 A:HIS156 4.3 31.7 1.0
CD2 A:HIS156 4.3 31.3 1.0
OE2 A:GLU209 4.3 31.6 1.0
CD2 A:HIS48 4.4 26.3 1.0
CA A:HIS156 4.4 25.9 1.0
N A:GLU157 4.4 27.9 1.0
NH1 A:ARG88 4.6 28.7 1.0
O A:HOH2016 4.7 30.5 1.0
CB A:GLU51 4.8 24.0 1.0
C A:GLU157 4.9 28.7 1.0
C A:HIS156 5.0 27.0 1.0
CA A:HIS48 5.0 24.1 1.0

Reference:

A.Maqbool, M.Herve, D.Mengin-Lecreulx, A.J.Wilkinson, G.H.Thomas. Mpaa Is A Murein-Tripeptide-Specific Zinc Carboxypeptidase That Functions As Part of A Catabolic Pathway For Peptidoglycan Derived Peptides in Gamma-Proteobacteria. Biochem.J. V. 448 329 2012.
ISSN: ISSN 0264-6021
PubMed: 22970852
DOI: 10.1042/BJ20121164
Page generated: Wed Dec 16 05:04:14 2020

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