Zinc in PDB 4xna: Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Beta Homolysine

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

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

Protein crystallography data

The structure of Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Beta Homolysine, PDB code: 4xna was solved by A.Addlagatta, R.Gumpena, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 2.40
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.330, 120.330, 170.919, 90.00, 90.00, 120.00
R / Rfree (%) 13.3 / 18

Other elements in 4xna:

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

Sodium (Na) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Beta Homolysine (pdb code 4xna). 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-Beta Homolysine, PDB code: 4xna:

Zinc binding site 1 out of 1 in 4xna

Go back to Zinc Binding Sites List in 4xna
Zinc binding site 1 out of 1 in the Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Beta Homolysine


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-Beta Homolysine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:18.2
occ:1.00
 OE1 A:GLU320 1.9 14.5 1.0
O A:B3K902 2.0 18.1 0.5
NE2 A:HIS297 2.1 14.3 1.0
NE2 A:HIS301 2.2 15.0 1.0
OXT A:B3K902 2.2 10.5 0.5
O A:B3K902 2.2 11.6 0.5
C A:B3K902 2.5 11.1 0.5
CD A:GLU320 2.7 15.2 1.0
C A:B3K902 2.7 17.6 0.5
OE2 A:GLU320 2.8 14.6 1.0
OXT A:B3K902 2.9 18.1 0.5
CE1 A:HIS297 3.0 14.1 1.0
CD2 A:HIS297 3.1 13.4 1.0
CD2 A:HIS301 3.1 15.1 1.0
CE1 A:HIS301 3.2 14.7 1.0
N A:B3K902 3.9 17.6 0.5
OH A:TYR381 3.9 15.0 1.0
CE2 A:TYR381 3.9 14.3 1.0
CA A:B3K902 4.0 17.9 0.5
CA A:B3K902 4.0 11.4 0.5
N A:B3K902 4.1 11.9 0.5
ND1 A:HIS297 4.1 14.7 1.0
CG A:GLU320 4.1 14.8 1.0
CG A:HIS297 4.2 13.3 1.0
CG A:HIS301 4.2 14.4 1.0
CZ A:TYR381 4.3 15.9 1.0
ND1 A:HIS301 4.3 15.3 1.0
OE1 A:GLU298 4.5 22.5 1.0
CB A:B3K902 4.5 18.4 0.5
OE1 A:GLU264 4.6 14.4 1.0
CG2 A:THR323 4.6 17.2 1.0
CB A:B3K902 4.6 11.9 0.5
CB A:GLU320 4.7 14.1 1.0
CA A:GLU320 4.7 14.0 1.0
CB A:THR323 4.8 16.6 1.0
O9 A:MLI920 4.8 54.5 1.0
CD2 A:TYR381 4.9 13.6 1.0
OE2 A:GLU298 5.0 21.9 1.0
CD A:GLU264 5.0 14.1 1.0
OE2 A:GLU264 5.0 13.4 1.0

Reference:

A.Addlagatta, R.Gumpena. Crystal Structure of E. Coli Aminopeptidase N in Complex with L-Beta Homolysin To Be Published.
Page generated: Wed Dec 16 05:55:11 2020

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