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Zinc in PDB 2afu: Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester

Enzymatic activity of Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester

All present enzymatic activity of Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester:
2.3.2.5;

Protein crystallography data

The structure of Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester, PDB code: 2afu was solved by K.F.Huang, Y.L.Liu, W.J.Cheng, T.P.Ko, A.H.J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.22
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 119.137, 119.137, 332.612, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 22.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester (pdb code 2afu). 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 Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester, PDB code: 2afu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2afu

Go back to Zinc Binding Sites List in 2afu
Zinc binding site 1 out of 2 in the Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester


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 Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn391

b:28.9
occ:1.00
OE2 A:GLU202 2.0 26.2 1.0
OD2 A:ASP159 2.0 28.7 1.0
N A:BGT381 2.1 41.4 1.0
NE2 A:HIS330 2.1 26.1 1.0
CD A:GLU202 2.8 24.9 1.0
O A:BGT381 2.9 43.5 1.0
CG A:ASP159 2.9 28.6 1.0
OE1 A:GLU202 2.9 24.4 1.0
CD2 A:HIS330 3.0 25.7 1.0
OD1 A:ASP159 3.1 29.1 1.0
CE1 A:HIS330 3.2 24.1 1.0
CA A:BGT381 3.3 42.6 1.0
C A:BGT381 3.5 43.0 1.0
O A:HOH533 4.0 22.8 1.0
CB A:BGT381 4.0 41.5 1.0
OE1 A:GLN201 4.1 29.6 1.0
CG A:HIS330 4.2 26.7 1.0
CG A:GLU202 4.2 24.6 1.0
ND1 A:HIS330 4.2 27.1 1.0
CB A:ASP159 4.3 27.2 1.0
NE1 A:TRP329 4.3 22.9 1.0
O A:HOH529 4.7 22.3 1.0
CD2 A:LEU249 4.7 25.4 1.0
OXT A:BGT381 4.7 43.1 1.0
CD1 A:TRP329 4.9 23.8 1.0
NE2 A:HIS140 4.9 25.3 1.0

Zinc binding site 2 out of 2 in 2afu

Go back to Zinc Binding Sites List in 2afu
Zinc binding site 2 out of 2 in the Crystal Structure of Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester


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 Human Glutaminyl Cyclase in Complex with Glutamine T-Butyl Ester within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn392

b:26.9
occ:1.00
OE2 B:GLU202 1.8 22.1 1.0
OD2 B:ASP159 1.9 25.2 1.0
NE2 B:HIS330 2.1 24.6 1.0
O B:HOH401 2.4 29.9 1.0
CD B:GLU202 2.7 21.6 1.0
CG B:ASP159 2.9 24.8 1.0
OE1 B:GLU202 2.9 22.0 1.0
CD2 B:HIS330 2.9 24.6 1.0
OD1 B:ASP159 3.1 24.4 1.0
CE1 B:HIS330 3.1 24.6 1.0
NE1 B:TRP329 4.0 22.6 1.0
CG B:GLU202 4.1 21.0 1.0
O B:HOH467 4.1 22.7 1.0
CG B:HIS330 4.1 25.5 1.0
ND1 B:HIS330 4.2 24.8 1.0
CB B:ASP159 4.2 23.4 1.0
OE1 B:BGT382 4.3 39.7 1.0
OE1 B:GLN201 4.4 28.7 1.0
O B:HOH463 4.5 27.4 1.0
CD2 B:LEU249 4.6 21.5 1.0
CE2 B:TRP329 4.7 23.2 1.0
CD1 B:TRP329 4.8 24.1 1.0
CZ2 B:TRP329 4.9 22.7 1.0
CD B:LYS144 5.0 20.8 1.0
NE2 B:HIS140 5.0 22.3 1.0
O B:HOH609 5.0 20.5 1.0

Reference:

K.F.Huang, Y.L.Liu, W.J.Cheng, T.P.Ko, A.H.Wang. Crystal Structures of Human Glutaminyl Cyclase, An Enzyme Responsible For Protein N-Terminal Pyroglutamate Formation Proc.Natl.Acad.Sci.Usa V. 102 13117 2005.
ISSN: ISSN 0027-8424
PubMed: 16135565
DOI: 10.1073/PNAS.0504184102
Page generated: Wed Dec 16 03:17:20 2020

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