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Zinc in PDB 1bpn: 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: 1bpn 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 (°) 129.800, 129.800, 120.700, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / n/a

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 1bpn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Differentiation and Identification of the Two Catalytic Metal Binding Sites in Bovine Lens Leucine Aminopeptidase By X-Ray Crystallography, PDB code: 1bpn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1bpn

Go back to Zinc Binding Sites List in 1bpn
Zinc binding site 1 out of 2 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:Zn488

b:8.9
occ:1.00
 OE1 A:GLU334 2.2 20.2 1.0
OD2 A:ASP255 2.2 14.2 1.0
OD1 A:ASP332 2.2 15.9 1.0
O A:ASP332 2.4 13.0 1.0
ZN A:ZN489 2.9 16.4 1.0
CG A:ASP255 3.0 3.7 1.0
CG A:ASP332 3.1 6.4 1.0
C A:ASP332 3.1 5.2 1.0
CD A:GLU334 3.2 18.8 1.0
OD1 A:ASP255 3.2 2.0 1.0
CA A:ASP332 3.3 4.4 1.0
OE2 A:GLU334 3.4 16.9 1.0
CB A:ASP332 3.6 6.9 1.0
OD2 A:ASP332 4.1 2.0 1.0
NZ A:LYS262 4.1 7.0 1.0
CE A:LYS262 4.3 4.0 1.0
N A:ALA333 4.4 5.2 1.0
CB A:ASP255 4.5 2.0 1.0
N A:GLU334 4.5 2.0 1.0
CG A:GLU334 4.6 14.7 1.0
OD1 A:ASN305 4.6 2.0 1.0
NH2 A:ARG336 4.6 15.7 1.0
N A:ASP332 4.7 4.6 1.0
OD2 A:ASP273 4.7 4.5 1.0
CA A:GLY257 4.8 2.0 1.0
O A:THR331 4.9 4.4 1.0
CA A:ALA333 4.9 2.0 1.0

Zinc binding site 2 out of 2 in 1bpn

Go back to Zinc Binding Sites List in 1bpn
Zinc binding site 2 out of 2 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 2 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:16.4
occ:1.00
 OD2 A:ASP273 2.2 4.5 1.0
OE2 A:GLU334 2.2 16.9 1.0
OD2 A:ASP255 2.2 14.2 1.0
NZ A:LYS250 2.3 8.2 1.0
ZN A:ZN488 2.9 8.9 1.0
CG A:ASP273 3.0 2.4 1.0
CD A:GLU334 3.0 18.8 1.0
OD1 A:ASP273 3.1 2.0 1.0
OE1 A:GLU334 3.3 20.2 1.0
CG A:ASP255 3.4 3.7 1.0
CE A:LYS250 3.7 2.0 1.0
CB A:ASP255 4.1 2.0 1.0
OD1 A:ASP255 4.3 2.0 1.0
CG1 A:ILE252 4.3 2.0 1.0
O A:ASP332 4.3 13.0 1.0
CB A:ASP273 4.4 3.9 1.0
CD A:LYS250 4.4 2.0 1.0
CG A:GLU334 4.4 14.7 1.0
O A:THR359 4.5 2.0 1.0
N A:GLY335 4.6 3.0 1.0
CB A:ILE252 4.8 2.0 1.0
NH1 A:ARG336 4.8 8.7 1.0
CE A:MET270 4.9 10.6 1.0
CA A:GLY335 4.9 2.0 1.0
NH2 A:ARG336 5.0 15.7 1.0
OD1 A:ASP332 5.0 15.9 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 02:45:57 2020

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