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Zinc in PDB 4q4i: Crystal Structure of E.Coli Aminopeptidase N in Complex with Amastatin

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

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

Protein crystallography data

The structure of Crystal Structure of E.Coli Aminopeptidase N in Complex with Amastatin, PDB code: 4q4i was solved by R.Reddi, R.J.Ganji, A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.72 / 2.31
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 119.386, 119.386, 170.129, 90.00, 90.00, 120.00
R / Rfree (%) 14 / 17.9

Other elements in 4q4i:

The structure of Crystal Structure of E.Coli Aminopeptidase N in Complex with Amastatin 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 Amastatin (pdb code 4q4i). 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 Amastatin, PDB code: 4q4i:

Zinc binding site 1 out of 1 in 4q4i

Go back to Zinc Binding Sites List in 4q4i
Zinc binding site 1 out of 1 in the Crystal Structure of E.Coli Aminopeptidase N in Complex with Amastatin


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 Amastatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:18.8
occ:1.00
 O1 C:L2O1 2.0 19.7 1.0
OE1 A:GLU320 2.0 16.2 1.0
NE2 A:HIS297 2.0 17.6 1.0
NE2 A:HIS301 2.1 17.6 1.0
O C:L2O1 2.5 25.1 1.0
CD A:GLU320 2.8 17.8 1.0
CD2 A:HIS297 2.9 19.5 1.0
OE2 A:GLU320 2.9 18.4 1.0
C6 C:L2O1 2.9 21.1 1.0
CD2 A:HIS301 3.0 17.4 1.0
C C:L2O1 3.0 21.6 1.0
CE1 A:HIS297 3.1 19.2 1.0
CE1 A:HIS301 3.2 17.0 1.0
C1 C:L2O1 3.6 18.4 1.0
N C:L2O1 3.7 19.0 1.0
OE1 A:GLU298 3.9 20.3 1.0
OH A:TYR381 4.0 18.1 1.0
CG A:HIS297 4.1 17.2 1.0
CE2 A:TYR381 4.2 16.0 1.0
ND1 A:HIS297 4.2 18.4 1.0
CG A:HIS301 4.2 18.5 1.0
ND1 A:HIS301 4.2 18.0 1.0
CG A:GLU320 4.3 17.6 1.0
N C:VAL2 4.3 20.7 1.0
OE2 A:GLU298 4.3 17.6 1.0
CZ A:TYR381 4.4 16.2 1.0
CD A:GLU298 4.5 18.6 1.0
OE1 A:GLU264 4.5 18.5 1.0
CG2 A:THR323 4.7 15.9 1.0
CA A:GLU320 4.8 17.3 1.0
CB A:GLU320 4.8 18.0 1.0
CB A:THR323 4.9 14.8 1.0
CD A:GLU264 4.9 18.6 1.0
OE2 A:GLU264 5.0 17.9 1.0

Reference:

R.J.Ganji, R.Reddi, R.Gumpena, A.K.Marapaka, T.Arya, P.Sankoju, S.Bhukya, A.Addlagatta. Structural Basis For the Inhibition of M1 Family Aminopeptidases By the Natural Product Actinonin: Crystal Structure in Complex with E. Coli Aminopeptidase N Protein Sci. 2015.
ISSN: ESSN 1469-896X
PubMed: 25644575
DOI: 10.1002/PRO.2653
Page generated: Wed Dec 16 05:42:31 2020

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