Zinc in PDB 4bin: Crystal Structure of the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic

Enzymatic activity of Crystal Structure of the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic

All present enzymatic activity of Crystal Structure of the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic:
3.5.1.28;

Protein crystallography data

The structure of Crystal Structure of the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic, PDB code: 4bin was solved by F.Kerff, M.Rocaboy, R.Herman, E.Sauvage, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 90.58 / 2.49
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.032, 68.442, 90.576, 90.00, 90.00, 90.00
R / Rfree (%) 17.564 / 23.101

Other elements in 4bin:

The structure of Crystal Structure of the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic (pdb code 4bin). 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 the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic, PDB code: 4bin:

Zinc binding site 1 out of 1 in 4bin

Go back to Zinc Binding Sites List in 4bin
Zinc binding site 1 out of 1 in the Crystal Structure of the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic


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 the E. Coli N-Acetylmuramoyl-L-Alanine Amidase Amic within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:34.5
occ:1.00
 OD1 A:ASP267 2.0 29.7 1.0
OE1 A:GLN299 2.0 39.1 1.0
OE2 A:GLU211 2.0 20.6 1.0
ND1 A:HIS265 2.2 27.8 1.0
NE2 A:HIS196 2.2 24.1 1.0
CD A:GLU211 2.8 26.8 1.0
CG A:ASP267 2.9 29.6 1.0
CD A:GLN299 2.9 35.7 1.0
OE1 A:GLU211 3.0 28.6 1.0
CD2 A:HIS196 3.1 27.1 1.0
CE1 A:HIS265 3.1 32.8 1.0
OD2 A:ASP267 3.2 31.3 1.0
CG A:HIS265 3.2 28.9 1.0
CE1 A:HIS196 3.3 17.6 1.0
O A:HOH2026 3.4 32.5 1.0
NE2 A:GLN299 3.4 26.6 1.0
CB A:HIS265 3.6 23.2 1.0
CG A:GLN299 4.2 27.9 1.0
CB A:ASP267 4.2 24.1 1.0
CG A:GLU211 4.2 20.2 1.0
NE2 A:HIS265 4.3 30.5 1.0
CG A:HIS196 4.3 33.9 1.0
CA A:HIS265 4.3 26.0 1.0
N A:ALA266 4.3 27.3 1.0
ND1 A:HIS196 4.3 24.1 1.0
CD2 A:HIS265 4.4 29.7 1.0
N A:ASP267 4.5 26.2 1.0
CA A:ASP267 4.5 26.0 1.0
O A:HOH2043 4.8 41.3 1.0
C A:ALA266 4.9 27.7 1.0
C A:HIS265 4.9 26.5 1.0

Reference:

M.Rocaboy, R.Herman, E.Sauvage, H.Remaut, K.Moonens, M.Terrak, P.Charlier, F.Kerff. The Crystal Structure of the Cell Division Amidase Amic Reveals the Fold of the Amin Domain, A New Peptidoglycan Binding Domain. Mol.Microbiol. V. 90 267 2013.
ISSN: ISSN 0950-382X
PubMed: 23927005
DOI: 10.1111/MMI.12361
Page generated: Wed Dec 16 05:05:20 2020

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