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Zinc in PDB 4fkk: Crystal Structure of Porcine Aminopeptidase-N Complexed with Bestatin

Enzymatic activity of Crystal Structure of Porcine Aminopeptidase-N Complexed with Bestatin

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

Protein crystallography data

The structure of Crystal Structure of Porcine Aminopeptidase-N Complexed with Bestatin, PDB code: 4fkk was solved by L.Chen, Y.L.Lin, G.Peng, F.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.28 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 260.611, 63.014, 81.705, 90.00, 100.83, 90.00
R / Rfree (%) 16.4 / 27.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Porcine Aminopeptidase-N Complexed with Bestatin (pdb code 4fkk). 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 Porcine Aminopeptidase-N Complexed with Bestatin, PDB code: 4fkk:

Zinc binding site 1 out of 1 in 4fkk

Go back to Zinc Binding Sites List in 4fkk
Zinc binding site 1 out of 1 in the Crystal Structure of Porcine 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 Porcine Aminopeptidase-N Complexed with Bestatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1025

b:27.2
occ:1.00
OE2 A:GLU406 2.0 21.3 1.0
NE2 A:HIS383 2.2 18.9 1.0
NE2 A:HIS387 2.2 25.8 1.0
O2 A:BES1024 2.2 51.6 1.0
CD A:GLU406 2.7 19.4 1.0
OE1 A:GLU406 2.8 16.5 1.0
CD2 A:HIS383 3.0 20.3 1.0
O3 A:BES1024 3.0 70.1 1.0
CD2 A:HIS387 3.0 26.7 1.0
C2 A:BES1024 3.2 68.2 1.0
CE1 A:HIS383 3.2 19.4 1.0
CE1 A:HIS387 3.3 25.4 1.0
C3 A:BES1024 3.4 69.1 1.0
N2 A:BES1024 3.8 53.0 1.0
C1 A:BES1024 3.9 69.1 1.0
OE1 A:GLU350 4.1 17.8 1.0
CG A:GLU406 4.2 17.8 1.0
CG A:HIS383 4.2 18.7 1.0
CG A:HIS387 4.2 26.1 1.0
OE2 A:GLU384 4.2 22.8 1.0
ND1 A:HIS383 4.3 20.3 1.0
ND1 A:HIS387 4.3 25.6 1.0
CB A:ALA409 4.3 12.5 1.0
CE2 A:TYR472 4.4 22.4 1.0
N1 A:BES1024 4.5 60.1 1.0
OE1 A:GLU384 4.6 16.4 1.0
CB A:GLU406 4.6 16.3 1.0
CD A:GLU350 4.7 17.0 1.0
CA A:GLU406 4.7 18.7 1.0
OH A:TYR472 4.8 30.5 1.0
CD A:GLU384 4.8 18.1 1.0
OE2 A:GLU350 4.9 16.2 1.0
O A:HOH1234 4.9 29.3 1.0

Reference:

L.Chen, Y.L.Lin, G.Peng, F.Li. Structural Basis For Multifunctional Roles of Mammalian Aminopeptidase N. Proc.Natl.Acad.Sci.Usa V. 109 17966 2012.
ISSN: ISSN 0027-8424
PubMed: 23071329
DOI: 10.1073/PNAS.1210123109
Page generated: Sat Oct 26 22:49:37 2024

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