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Zinc in PDB 3fh4: Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase

Enzymatic activity of Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase

All present enzymatic activity of Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase:
3.4.11.10;

Protein crystallography data

The structure of Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase, PDB code: 3fh4 was solved by W.Yong, J.-J.P.Kim, M.Hartley, B.Bennett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.03 / 1.95
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 108.397, 108.397, 93.529, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / 22.8

Other elements in 3fh4:

The structure of Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase (pdb code 3fh4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase, PDB code: 3fh4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3fh4

Go back to Zinc Binding Sites List in 3fh4
Zinc binding site 1 out of 2 in the Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase


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 Recombinant Vibrio Proteolyticus Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:15.5
occ:1.00
OD2 A:ASP117 2.1 9.5 1.0
NE2 A:HIS256 2.1 10.8 1.0
OE2 A:GLU152 2.2 10.2 1.0
O1 A:TRS302 2.2 18.6 1.0
N A:TRS302 2.3 18.8 1.0
OE1 A:GLU152 2.4 11.4 1.0
CD A:GLU152 2.6 11.7 1.0
CG A:ASP117 3.0 11.6 1.0
CE1 A:HIS256 3.1 12.9 1.0
CD2 A:HIS256 3.1 11.6 1.0
C A:TRS302 3.2 19.6 1.0
C1 A:TRS302 3.2 19.4 1.0
OD1 A:ASP117 3.3 12.8 1.0
ZN A:ZN301 3.4 13.1 1.0
C2 A:TRS302 3.7 19.9 1.0
O2 A:TRS302 3.9 22.6 1.0
O A:HOH407 4.0 19.3 1.0
O A:HOH354 4.1 6.8 1.0
CG A:GLU152 4.1 10.9 1.0
OE1 A:GLU151 4.2 11.5 1.0
ND1 A:HIS256 4.2 14.3 1.0
CG A:HIS256 4.3 13.3 1.0
CB A:ASP117 4.3 11.4 1.0
C3 A:TRS302 4.5 19.2 1.0
NE2 A:HIS97 4.6 10.2 1.0
CE1 A:HIS97 4.7 9.5 1.0
CD1 A:ILE255 4.7 13.8 1.0
O3 A:TRS302 4.9 18.5 1.0
CG2 A:THR101 5.0 13.2 1.0

Zinc binding site 2 out of 2 in 3fh4

Go back to Zinc Binding Sites List in 3fh4
Zinc binding site 2 out of 2 in the Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Recombinant Vibrio Proteolyticus Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:13.1
occ:1.00
OD1 A:ASP117 1.9 12.8 1.0
OD1 A:ASP179 2.1 13.1 1.0
NE2 A:HIS97 2.1 10.2 1.0
O1 A:TRS302 2.1 18.6 1.0
OD2 A:ASP179 2.4 13.6 1.0
CG A:ASP179 2.6 12.3 1.0
O2 A:TRS302 2.8 22.6 1.0
CG A:ASP117 3.0 11.6 1.0
C1 A:TRS302 3.0 19.4 1.0
CE1 A:HIS97 3.0 9.5 1.0
CD2 A:HIS97 3.1 11.1 1.0
OD2 A:ASP117 3.4 9.5 1.0
ZN A:ZN300 3.4 15.5 1.0
OE1 A:GLU151 3.5 11.5 1.0
OE2 A:GLU152 3.7 10.2 1.0
C2 A:TRS302 3.9 19.9 1.0
C A:TRS302 3.9 19.6 1.0
CB A:ASP118 4.0 10.8 1.0
CB A:ASP179 4.1 10.6 1.0
CD A:GLU151 4.1 12.1 1.0
ND1 A:HIS97 4.2 10.1 1.0
CG A:HIS97 4.2 10.2 1.0
CB A:ASP117 4.3 11.4 1.0
N A:TRS302 4.4 18.8 1.0
CD A:GLU152 4.4 11.7 1.0
OE2 A:GLU151 4.4 11.6 1.0
CA A:ASP117 4.5 11.3 1.0
CG A:ASP118 4.6 11.3 1.0
OE1 A:GLU152 4.7 11.4 1.0
C A:ASP117 4.7 11.1 1.0
OG A:SER228 4.8 11.1 1.0
CA A:ASP179 4.8 10.9 1.0
N A:ASP118 4.8 11.1 1.0
CA A:ASP118 4.9 11.0 1.0
OD2 A:ASP118 4.9 10.9 1.0
CG A:MET180 4.9 10.4 1.0
C A:ASP179 5.0 10.8 1.0

Reference:

M.Hartley, B.Bennett. Heterologous Expression and Purification of Vibrio Proteolyticus (Aeromonas Proteolytica) Aminopeptidase: A Rapid Protocol Protein Expr.Purif. V. 66 91 2009.
ISSN: ISSN 1046-5928
PubMed: 19233285
DOI: 10.1016/J.PEP.2009.02.011
Page generated: Thu Oct 24 13:11:22 2024

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