Zinc in PDB 2zxg: Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue

Enzymatic activity of Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue

All present enzymatic activity of Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue:
3.4.11.2;

Protein crystallography data

The structure of Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue, PDB code: 2zxg was solved by Y.Nakajima, K.Ito, T.Yoshimoto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.55
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.700, 120.700, 171.000, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 19.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue (pdb code 2zxg). 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 Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue, PDB code: 2zxg:

Zinc binding site 1 out of 1 in 2zxg

Go back to Zinc Binding Sites List in 2zxg
Zinc binding site 1 out of 1 in the Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aminopeptidase N Complexed with the Aminophosphinic Inhibitor of PL250, A Transition State Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn900

b:10.0
occ:1.00
 OE2 A:GLU320 2.0 9.3 1.0
O1 A:S23901 2.0 12.0 1.0
NE2 A:HIS297 2.0 9.5 1.0
NE2 A:HIS301 2.1 8.1 1.0
CD A:GLU320 2.8 10.1 1.0
OE1 A:GLU320 2.9 10.2 1.0
O2 A:S23901 2.9 13.1 1.0
CE1 A:HIS301 3.0 8.4 1.0
CD2 A:HIS297 3.0 9.7 1.0
CE1 A:HIS297 3.0 10.0 1.0
P A:S23901 3.0 2.0 1.0
CD2 A:HIS301 3.1 9.9 1.0
N1 A:S23901 3.7 9.6 1.0
C1 A:S23901 4.0 10.7 1.0
CE2 A:TYR381 4.0 11.2 1.0
OH A:TYR381 4.0 11.9 1.0
ND1 A:HIS301 4.1 8.6 1.0
ND1 A:HIS297 4.1 10.1 1.0
CG A:HIS297 4.2 8.6 1.0
CG A:HIS301 4.2 9.1 1.0
CG A:GLU320 4.2 8.7 1.0
C3 A:S23901 4.3 13.3 1.0
CZ A:TYR381 4.4 11.2 1.0
C4 A:S23901 4.5 12.5 1.0
OE2 A:GLU264 4.6 9.3 1.0
CG2 A:THR323 4.6 9.8 1.0
CB A:THR323 4.7 8.7 1.0
CB A:GLU320 4.8 9.0 1.0
CA A:GLU320 4.8 9.1 1.0
C2 A:S23901 4.9 12.0 1.0
OE2 A:GLU298 4.9 12.0 1.0
CD2 A:TYR381 5.0 11.5 1.0

Reference:

M.C.Fournie-Zaluski, H.Poras, B.P.Roques, Y.Nakajima, K.Ito, T.Yoshimoto. Structure of Aminopeptidase N From Escherichia Coli Complexed with the Transition-State Analogue Aminophosphinic Inhibitor PL250 Acta Crystallogr.,Sect.D V. 65 814 2009.
ISSN: ISSN 0907-4449
PubMed: 19622865
DOI: 10.1107/S090744490901779X
Page generated: Thu Oct 24 10:59:55 2024

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