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Zinc in PDB 2dq6: Crystal Structure of Aminopeptidase N From Escherichia Coli

Enzymatic activity of Crystal Structure of Aminopeptidase N From Escherichia Coli

All present enzymatic activity of Crystal Structure of Aminopeptidase N From Escherichia Coli:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of Aminopeptidase N From Escherichia Coli, PDB code: 2dq6 was solved by Y.Nakajima, Y.Onohara, 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 / 1.50
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.480, 120.480, 170.791, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 19.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Aminopeptidase N From Escherichia Coli (pdb code 2dq6). 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 From Escherichia Coli, PDB code: 2dq6:

Zinc binding site 1 out of 1 in 2dq6

Go back to Zinc Binding Sites List in 2dq6
Zinc binding site 1 out of 1 in the Crystal Structure of Aminopeptidase N From Escherichia Coli


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 From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn900

b:12.5
occ:1.00
OE2 A:GLU320 2.0 10.6 1.0
NE2 A:HIS301 2.1 8.3 1.0
NE2 A:HIS297 2.1 9.2 1.0
O A:HOH1001 2.2 20.8 1.0
CD A:GLU320 2.8 11.9 1.0
OE1 A:GLU320 2.9 12.1 1.0
CD2 A:HIS297 3.0 9.9 1.0
CD2 A:HIS301 3.0 9.6 1.0
CE1 A:HIS301 3.1 8.5 1.0
CE1 A:HIS297 3.1 9.2 1.0
O A:HOH1002 3.9 12.8 1.0
CE2 A:TYR381 4.0 12.5 1.0
OH A:TYR381 4.1 14.6 1.0
CG A:HIS297 4.2 8.5 1.0
CG A:HIS301 4.2 7.9 1.0
ND1 A:HIS301 4.2 7.8 1.0
O A:HOH1561 4.2 29.2 1.0
ND1 A:HIS297 4.2 9.4 1.0
CG A:GLU320 4.3 10.5 1.0
OE1 A:GLU298 4.3 17.4 1.0
CZ A:TYR381 4.4 11.5 1.0
OE2 A:GLU264 4.4 9.9 1.0
CG2 A:THR323 4.5 8.7 1.0
CA A:GLU320 4.7 8.5 1.0
CB A:THR323 4.7 9.0 1.0
OE2 A:GLU298 4.8 14.6 1.0
CB A:GLU320 4.8 9.6 1.0
O A:HOH1361 4.8 23.5 1.0
CD2 A:TYR381 4.9 10.6 1.0
CD A:GLU264 4.9 9.9 1.0
CD A:GLU298 5.0 14.2 1.0
OE1 A:GLU264 5.0 9.7 1.0

Reference:

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
Page generated: Wed Dec 16 03:22:05 2020

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