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Zinc in PDB 3pb8: Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine:
2.3.2.5;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine, PDB code: 3pb8 was solved by K.F.Huang, S.S.Liaw, W.L.Huang, C.Y.Chia, Y.C.Lo, Y.L.Chen, 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 / 1.13
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.301, 68.580, 77.439, 90.00, 90.00, 90.00
R / Rfree (%) 13.1 / 16.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine (pdb code 3pb8). 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 the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine, PDB code: 3pb8:

Zinc binding site 1 out of 1 in 3pb8

Go back to Zinc Binding Sites List in 3pb8
Zinc binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine


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 the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase in Complex with N-Acetylhistamine within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Zn400

b:7.7
occ:1.00
 OE2 X:GLU226 1.9 8.1 1.0
NE2 X:AHN390 2.0 8.4 1.0
OD2 X:ASP186 2.0 7.8 1.0
NE2 X:HIS351 2.0 7.6 1.0
CG X:ASP186 2.7 6.5 1.0
CD X:GLU226 2.8 7.6 1.0
OD1 X:ASP186 2.8 7.6 1.0
OE1 X:GLU226 2.9 9.0 1.0
CE1 X:AHN390 3.0 8.7 1.0
CD2 X:HIS351 3.0 8.2 1.0
CD2 X:AHN390 3.0 11.3 1.0
CE1 X:HIS351 3.0 8.1 1.0
ND1 X:AHN390 4.1 9.9 1.0
NE1 X:TRP350 4.1 9.3 1.0
O X:HOH408 4.1 8.2 1.0
CG X:AHN390 4.1 11.3 1.0
CG X:HIS351 4.1 8.2 1.0
ND1 X:HIS351 4.2 8.8 1.0
CG X:GLU226 4.2 8.7 1.0
CB X:ASP186 4.2 7.9 1.0
O X:HOH540 4.2 14.5 1.0
OE1 X:GLU225 4.4 11.3 1.0
O X:HOH409 4.5 8.4 1.0
NE2 X:HIS168 4.7 7.5 1.0
CD2 X:LEU270 4.7 8.8 1.0
CD1 X:TRP350 4.7 9.2 1.0
CE2 X:TRP350 4.8 9.7 1.0
CD X:LYS172 4.9 11.3 1.0
O X:ASP186 5.0 8.0 1.0
CE1 X:HIS168 5.0 7.6 1.0

Reference:

K.F.Huang, S.S.Liaw, W.L.Huang, C.Y.Chia, Y.C.Lo, Y.L.Chen, A.H.J.Wang. Structures of Human Golgi-Resident Glutaminyl Cyclase and Its Complexes with Inhibitors Reveal A Large Loop Movement Upon Inhibitor Binding J.Biol.Chem. V. 286 12439 2011.
ISSN: ISSN 0021-9258
PubMed: 21288892
DOI: 10.1074/JBC.M110.208595
Page generated: Sat Oct 26 11:22:12 2024

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