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Zinc in PDB 2wkx: Crystal Structure of the Native E. Coli Zinc Amidase Amid

Enzymatic activity of Crystal Structure of the Native E. Coli Zinc Amidase Amid

All present enzymatic activity of Crystal Structure of the Native E. Coli Zinc Amidase Amid:
3.5.1.28;

Protein crystallography data

The structure of Crystal Structure of the Native E. Coli Zinc Amidase Amid, PDB code: 2wkx was solved by S.Petrella, F.Kerff, R.Herman, C.Genereux, A.Pennartz, E.Sauvage, B.Joris, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.23 / 1.80
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 88.990, 88.990, 183.923, 90.00, 90.00, 120.00
R / Rfree (%) 16.077 / 18.367

Other elements in 2wkx:

The structure of Crystal Structure of the Native E. Coli Zinc Amidase Amid also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Native E. Coli Zinc Amidase Amid (pdb code 2wkx). 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 Native E. Coli Zinc Amidase Amid, PDB code: 2wkx:

Zinc binding site 1 out of 1 in 2wkx

Go back to Zinc Binding Sites List in 2wkx
Zinc binding site 1 out of 1 in the Crystal Structure of the Native E. Coli Zinc Amidase Amid


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 Native E. Coli Zinc Amidase Amid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:11.2
occ:1.00
OD1 A:ASP161 1.9 8.3 1.0
ND1 A:HIS151 2.1 7.1 1.0
ND1 A:HIS35 2.1 6.8 1.0
CL A:CL302 2.3 28.9 1.0
CG A:ASP161 2.8 8.2 1.0
OD2 A:ASP161 3.0 5.5 1.0
CG A:HIS151 3.0 7.1 1.0
CE1 A:HIS35 3.1 6.0 1.0
CE1 A:HIS151 3.1 8.2 1.0
CG A:HIS35 3.2 6.5 1.0
CB A:HIS151 3.3 6.6 1.0
CB A:HIS35 3.5 6.5 1.0
CA A:HIS35 4.1 7.6 1.0
CD2 A:HIS151 4.2 6.9 1.0
NE2 A:HIS151 4.2 6.6 1.0
NE2 A:HIS35 4.2 6.4 1.0
CB A:ASP161 4.3 7.0 1.0
CD2 A:HIS35 4.3 7.1 1.0
O A:HOH2091 4.4 29.1 1.0
O A:HOH2139 4.4 32.4 1.0
O A:HIS84 4.6 8.8 1.0
O A:TYR36 4.6 6.8 1.0
OE2 A:GLU104 4.6 16.1 1.0
O A:HOH2070 4.7 30.7 1.0
CD A:LYS159 4.7 12.6 1.0
CA A:HIS151 4.8 6.1 1.0
N A:TYR36 4.8 6.4 1.0
CE A:LYS159 4.9 16.9 1.0
CG A:LYS159 4.9 7.0 1.0
NZ A:LYS159 5.0 14.4 1.0

Reference:

F.Kerff, S.Petrella, F.Mercier, E.Sauvage, R.Herman, A.Pennartz, A.Zervosen, A.Luxen, J.M.Frere, B.Joris, P.Charlier. Specific Structural Features of the N- Acetylmuramoyl-L-Alanine Amidase Amid From Escherichia Coli and Mechanistic Implications For Enzymes of This Family. J.Mol.Biol. V. 397 249 2010.
ISSN: ISSN 0022-2836
PubMed: 20036252
DOI: 10.1016/J.JMB.2009.12.038
Page generated: Thu Oct 17 04:56:31 2024

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