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Zinc in PDB 1bpm: Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography

Enzymatic activity of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography

All present enzymatic activity of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography:
3.4.11.1;

Protein crystallography data

The structure of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography, PDB code: 1bpm was solved by H.Kim, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.90
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 129.100, 129.100, 120.200, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / n/a

Other elements in 1bpm:

The structure of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography (pdb code 1bpm). 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 Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography, PDB code: 1bpm:

Zinc binding site 1 out of 1 in 1bpm

Go back to Zinc Binding Sites List in 1bpm
Zinc binding site 1 out of 1 in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn489

b:16.8
occ:1.00
 OD2 A:ASP273 2.2 5.1 1.0
OD2 A:ASP255 2.2 11.5 1.0
OE2 A:GLU334 2.2 15.8 1.0
NZ A:LYS250 2.3 7.0 1.0
MG A:MG488 2.6 4.6 1.0
OE1 A:GLU334 2.7 13.8 1.0
CD A:GLU334 2.7 15.7 1.0
CG A:ASP273 3.0 5.7 1.0
OD1 A:ASP273 3.1 3.2 1.0
CG A:ASP255 3.3 5.4 1.0
CE A:LYS250 3.7 6.4 1.0
CB A:ASP255 3.9 2.8 1.0
OD1 A:ASP255 4.2 7.9 1.0
CG A:GLU334 4.2 8.3 1.0
O A:ASP332 4.2 7.7 1.0
CB A:ASP273 4.4 2.0 1.0
CG1 A:ILE252 4.5 2.1 1.0
O A:THR359 4.6 2.0 1.0
CD A:LYS250 4.7 2.0 1.0
OD1 A:ASP332 4.7 10.9 1.0
N A:GLY335 4.7 6.0 1.0
CB A:ILE252 4.8 3.9 1.0
CG2 A:ILE252 4.9 2.0 1.0
O A:LEU360 5.0 14.8 1.0

Reference:

H.Kim, W.N.Lipscomb. Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography. Proc.Natl.Acad.Sci.Usa V. 90 5006 1993.
ISSN: ISSN 0027-8424
PubMed: 8506345
DOI: 10.1073/PNAS.90.11.5006
Page generated: Wed Dec 16 02:45:56 2020

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