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Zinc in PDB 3puu: Crystal Structure of GLU121GLN Mutant of E. Coli Aminopeptidase N

Enzymatic activity of Crystal Structure of GLU121GLN Mutant of E. Coli Aminopeptidase N

All present enzymatic activity of Crystal Structure of GLU121GLN Mutant of E. Coli Aminopeptidase N:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of GLU121GLN Mutant of E. Coli Aminopeptidase N, PDB code: 3puu was solved by A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.33 / 2.15
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.764, 120.764, 170.844, 90.00, 90.00, 120.00
R / Rfree (%) 15.2 / 18.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of GLU121GLN Mutant of E. Coli Aminopeptidase N (pdb code 3puu). 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 GLU121GLN Mutant of E. Coli Aminopeptidase N, PDB code: 3puu:

Zinc binding site 1 out of 1 in 3puu

Go back to Zinc Binding Sites List in 3puu
Zinc binding site 1 out of 1 in the Crystal Structure of GLU121GLN Mutant of E. Coli Aminopeptidase N


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 GLU121GLN Mutant of E. Coli Aminopeptidase N within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn950

b:26.6
occ:0.50
OE1 A:GLU320 2.0 16.4 1.0
NE2 A:HIS301 2.1 11.4 1.0
NE2 A:HIS297 2.1 12.8 1.0
O A:HOH1578 2.6 39.6 1.0
O A:HOH1512 2.6 31.5 1.0
CD A:GLU320 2.8 12.7 1.0
OE2 A:GLU320 2.8 14.3 1.0
CD2 A:HIS301 3.0 8.5 1.0
CD2 A:HIS297 3.1 10.9 1.0
CE1 A:HIS297 3.2 12.4 1.0
CE1 A:HIS301 3.2 9.2 1.0
OH A:TYR381 3.9 17.1 1.0
CE2 A:TYR381 4.0 13.9 1.0
CG A:HIS301 4.2 9.9 1.0
CG A:GLU320 4.2 10.3 1.0
CG A:HIS297 4.2 12.6 1.0
ND1 A:HIS301 4.2 9.7 1.0
ND1 A:HIS297 4.3 11.6 1.0
CZ A:TYR381 4.3 14.3 1.0
OE1 A:GLU298 4.4 18.6 1.0
OE1 A:GLU264 4.7 11.2 1.0
CA A:GLU320 4.7 10.1 1.0
OE2 A:GLU298 4.7 19.6 1.0
CB A:GLU320 4.8 9.4 1.0
CG2 A:THR323 4.8 9.1 1.0
NZ A:LYS319 4.9 8.0 1.0
OE2 A:GLU264 4.9 14.6 1.0
CB A:THR323 4.9 10.4 1.0
CD A:GLU298 5.0 17.1 1.0
CD A:GLU264 5.0 14.4 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: Sat Oct 26 11:47:57 2024

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