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Zinc in PDB 3qjx: Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Serine

Enzymatic activity of Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Serine

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

Protein crystallography data

The structure of Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Serine, PDB code: 3qjx was solved by A.Addlagatta, R.Gumpena, C.Kishor, R.J.Ganji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.74 / 1.45
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.230, 120.230, 170.801, 90.00, 90.00, 120.00
R / Rfree (%) 12 / 14.7

Other elements in 3qjx:

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

Sodium (Na) 3 atoms

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 3qjx

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


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 L-Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn880

b:6.6
occ:1.00
 OE1 A:GLU320 1.9 6.2 1.0
OXT A:SER900 1.9 8.2 1.0
NE2 A:HIS297 2.0 6.3 1.0
NE2 A:HIS301 2.0 5.0 1.0
CD A:GLU320 2.7 7.3 1.0
OE2 A:GLU320 2.8 6.9 1.0
C A:SER900 2.9 7.1 1.0
CE1 A:HIS301 2.9 6.2 1.0
CD2 A:HIS297 3.0 6.5 1.0
CE1 A:HIS297 3.0 7.7 1.0
CD2 A:HIS301 3.1 5.9 1.0
O A:SER900 3.5 9.6 1.0
CE2 A:TYR381 3.8 6.5 1.0
N A:SER900 3.9 7.9 1.0
OH A:TYR381 4.0 7.6 1.0
CA A:SER900 4.0 7.5 1.0
ND1 A:HIS301 4.1 5.6 1.0
CG A:HIS297 4.1 5.2 1.0
ND1 A:HIS297 4.1 6.9 1.0
CG A:HIS301 4.2 5.0 1.0
CG A:GLU320 4.2 5.8 1.0
CZ A:TYR381 4.3 6.8 1.0
CG2 A:THR323 4.5 6.5 1.0
O2 A:GOL976 4.5 20.4 0.5
OE1 A:GLU298 4.6 8.0 1.0
CB A:THR323 4.6 5.2 1.0
CA A:GLU320 4.6 5.3 1.0
OE1 A:GLU264 4.6 7.0 1.0
CB A:GLU320 4.7 5.6 1.0
CD2 A:TYR381 4.8 7.1 1.0

Reference:

R.Gumpena, C.Kishor, R.J.Ganji, A.Addlagatta. Discovery of Alpha, Beta- and Alpha, Gamma-Diamino Acid Scaffolds For the Inhibition of M1 Family Aminopeptidases Chemmedchem V. 6 1971 2011.
ISSN: ISSN 1860-7179
PubMed: 22025387
DOI: 10.1002/CMDC.201100298
Page generated: Wed Dec 16 04:45:21 2020

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