Zinc in PDB 2dqm: Crystal Structure of Aminopeptidase N Complexed with Bestatin

All present enzymatic activity of Crystal Structure of Aminopeptidase N Complexed with Bestatin:
3.4.11.2;

The structure of Crystal Structure of Aminopeptidase N Complexed with Bestatin, PDB code: 2dqm was solved by Y.Onohara, 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 / 1.60
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.417, 120.417, 170.859, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 19.4

The binding sites of Zinc atom in the Crystal Structure of Aminopeptidase N Complexed with Bestatin (pdb code 2dqm). 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 Aminopeptidase N Complexed with Bestatin, PDB code: 2dqm:

Zinc binding site 1 out of 1 in the Crystal Structure of Aminopeptidase N Complexed 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 Aminopeptidase N Complexed with Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn900 b:9.2 occ:1.00 OE1 A:GLU320 2.1 9.1 1.0 NE2 A:HIS297 2.1 8.4 1.0 NE2 A:HIS301 2.1 8.3 1.0 O2 A:BES901 2.2 16.5 1.0 O3 A:BES901 2.6 22.2 1.0 CD A:GLU320 2.8 9.8 1.0 OE2 A:GLU320 2.9 8.9 1.0 CD2 A:HIS297 3.0 9.9 1.0 CD2 A:HIS301 3.0 9.8 1.0 C2 A:BES901 3.1 15.9 1.0 C3 A:BES901 3.1 19.6 1.0 CE1 A:HIS301 3.1 8.4 1.0 CE1 A:HIS297 3.2 8.3 1.0 C1 A:BES901 3.7 15.8 1.0 N2 A:BES901 3.8 10.5 1.0 OH A:TYR381 4.1 10.3 1.0 CE2 A:TYR381 4.2 10.1 1.0 CG A:HIS297 4.2 8.1 1.0 CG A:HIS301 4.2 8.6 1.0 OE1 A:GLU298 4.2 12.7 1.0 ND1 A:HIS301 4.2 8.9 1.0 ND1 A:HIS297 4.2 8.4 1.0 CG A:GLU320 4.3 8.3 1.0 N1 A:BES901 4.3 19.5 1.0 CZ A:TYR381 4.5 9.6 1.0 OE2 A:GLU264 4.5 8.5 1.0 OE2 A:GLU298 4.6 11.1 1.0 CG2 A:THR323 4.6 8.5 1.0 CA A:GLU320 4.7 7.7 1.0 CB A:THR323 4.8 8.8 1.0 CD A:GLU298 4.8 12.6 1.0 C16 A:BES901 4.8 21.3 1.0 CB A:GLU320 4.8 8.2 1.0 C14 A:BES901 4.9 21.0 1.0 CD A:GLU264 5.0 9.1 1.0 OE1 A:GLU264 5.0 10.7 1.0

K.Ito, Y.Nakajima, Y.Onohara, M.Takeo, K.Nakashima, F.Matsubara, T.Ito, T.Yoshimoto. Aminopeptidase N (Proteobacteria Alanyl Aminopeptidase) From Escherichia Coli: Crystal Structure and Conformational Change of the Methionine 260 Residue Involved in Substrate Recognition J.Biol.Chem. V. 281 33664 2006.
ISSN: ISSN 0021-9258
PubMed: 16885166
DOI: 10.1074/JBC.M605203200