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Zinc in PDB 3b34: Crystal Structure of E. Coli Aminopeptidase N in Complex with Phenylalanine

Enzymatic activity of Crystal Structure of E. Coli Aminopeptidase N in Complex with Phenylalanine

All present enzymatic activity of Crystal Structure of E. Coli Aminopeptidase N in Complex with Phenylalanine:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of E. Coli Aminopeptidase N in Complex with Phenylalanine, PDB code: 3b34 was solved by A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.582, 120.582, 170.761, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 19.4

Other elements in 3b34:

The structure of Crystal Structure of E. Coli Aminopeptidase N in Complex with Phenylalanine also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of E. Coli Aminopeptidase N in Complex with Phenylalanine (pdb code 3b34). 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 E. Coli Aminopeptidase N in Complex with Phenylalanine, PDB code: 3b34:

Zinc binding site 1 out of 1 in 3b34

Go back to Zinc Binding Sites List in 3b34
Zinc binding site 1 out of 1 in the Crystal Structure of E. Coli Aminopeptidase N in Complex with Phenylalanine


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 E. Coli Aminopeptidase N in Complex with Phenylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn950

b:10.6
occ:1.00
 OXT A:PHE900 1.7 9.4 0.3
OE1 A:GLU320 1.9 10.8 1.0
NE2 A:HIS301 2.0 10.6 1.0
NE2 A:HIS297 2.0 9.7 1.0
O A:PHE900 2.1 14.9 0.7
C A:PHE900 2.7 14.8 0.7
OXT A:PHE900 2.7 14.9 0.7
CD A:GLU320 2.7 10.7 1.0
C A:PHE900 2.8 9.8 0.3
OE2 A:GLU320 2.9 11.9 1.0
CE1 A:HIS301 3.0 8.9 1.0
CD2 A:HIS297 3.0 10.0 1.0
CD2 A:HIS301 3.0 8.6 1.0
CE1 A:HIS297 3.0 10.2 1.0
O A:PHE900 3.3 9.0 0.3
CE2 A:TYR381 3.9 12.5 1.0
OH A:TYR381 4.0 14.0 1.0
CA A:PHE900 4.0 9.9 0.3
N A:PHE900 4.0 9.7 0.3
ND1 A:HIS301 4.1 10.1 1.0
ND1 A:HIS297 4.1 10.8 1.0
CG A:HIS297 4.1 9.2 1.0
CA A:PHE900 4.1 14.7 0.7
CG A:HIS301 4.1 9.5 1.0
CG A:GLU320 4.2 11.2 1.0
CZ A:TYR381 4.3 12.5 1.0
N A:PHE900 4.5 15.1 0.7
CG2 A:THR323 4.5 9.8 1.0
CB A:THR323 4.6 8.1 1.0
OE1 A:GLU264 4.6 10.6 1.0
CA A:GLU320 4.7 10.6 1.0
CB A:GLU320 4.8 11.1 1.0
OE1 A:GLU298 4.8 15.2 1.0
O1 A:GOL972 4.9 40.0 1.0
CD2 A:TYR381 4.9 10.2 1.0
CB A:PHE900 4.9 9.9 0.3
OE2 A:GLU264 4.9 10.9 1.0
CB A:PHE900 4.9 14.2 0.7
CD A:GLU264 5.0 9.8 1.0

Reference:

A.Addlagatta, L.Gay, B.W.Matthews. Structural Basis For the Unusual Specificity of Escherichia Coli Aminopeptidase N. Biochemistry V. 47 5303 2008.
ISSN: ISSN 0006-2960
PubMed: 18416562
DOI: 10.1021/BI7022333
Page generated: Thu Oct 24 11:23:18 2024

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