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Zinc in PDB 4xmx: Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin

Enzymatic activity of Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin

All present enzymatic activity of Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin, PDB code: 4xmx was solved by A.Addlagatta, R.Gumpena, C.Kishor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.81 / 2.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 121.037, 121.037, 170.658, 90.00, 90.00, 120.00
R / Rfree (%) 14.5 / 19.1

Other elements in 4xmx:

The structure of Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin also contains other interesting chemical elements:

Sodium (Na) 5 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin (pdb code 4xmx). 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 MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin, PDB code: 4xmx:

Zinc binding site 1 out of 1 in 4xmx

Go back to Zinc Binding Sites List in 4xmx
Zinc binding site 1 out of 1 in the Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin


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 MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:15.9
occ:1.00
O2 A:BES902 2.0 17.6 1.0
NE2 A:HIS297 2.0 14.7 1.0
OE1 A:GLU320 2.0 15.8 1.0
NE2 A:HIS301 2.1 15.9 1.0
O3 A:BES902 2.5 36.2 1.0
CD A:GLU320 2.7 14.0 1.0
OE2 A:GLU320 2.8 13.4 1.0
CD2 A:HIS297 3.0 13.8 1.0
CD2 A:HIS301 3.0 15.1 1.0
CE1 A:HIS297 3.0 15.6 1.0
C2 A:BES902 3.1 20.5 1.0
C3 A:BES902 3.1 28.0 1.0
CE1 A:HIS301 3.2 17.6 1.0
C1 A:BES902 3.7 20.9 1.0
N2 A:BES902 3.8 18.8 1.0
OH A:TYR381 4.0 16.3 1.0
OE1 A:GLU298 4.0 17.2 1.0
ND1 A:HIS297 4.1 15.8 1.0
CG A:HIS297 4.1 14.3 1.0
CG A:GLU320 4.2 14.3 1.0
CE2 A:TYR381 4.2 15.6 1.0
CG A:HIS301 4.2 15.1 1.0
ND1 A:HIS301 4.3 16.4 1.0
N1 A:BES902 4.3 29.6 1.0
CZ A:TYR381 4.5 15.4 1.0
OE1 A:GLU264 4.5 12.1 1.0
OE2 A:GLU298 4.6 19.4 1.0
CD A:GLU298 4.7 19.2 1.0
CB A:GLU320 4.7 14.2 1.0
CA A:GLU320 4.8 13.9 1.0
CG2 A:THR323 4.8 16.6 1.0
CB A:THR323 4.8 16.7 1.0
CD A:GLU264 4.9 13.4 1.0
OE2 A:GLU264 4.9 13.8 1.0
C14 A:BES902 5.0 26.1 1.0

Reference:

A.Addlagatta, R.Gumpena, C.Kishor. Crystal Structure of MET260ALA Mutant of E. Coli Aminopeptidase N in Complex with Bestatin To Be Published.
Page generated: Sun Oct 27 10:41:17 2024

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