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Arsenic in PDB 3pb6: Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5:
2.3.2.5;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5, PDB code: 3pb6 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 / 1.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.097, 68.527, 77.348, 90.00, 90.00, 90.00
R / Rfree (%) 13.8 / 15.8

Other elements in 3pb6:

The structure of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5 (pdb code 3pb6). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5, PDB code: 3pb6:

Arsenic binding site 1 out of 1 in 3pb6

Go back to Arsenic Binding Sites List in 3pb6
Arsenic binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of the Catalytic Domain of Human Golgi-Resident Glutaminyl Cyclase at pH 6.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
X:As390

b:8.2
occ:1.00
AS X:CAC390 0.0 8.2 1.0
O1 X:CAC390 1.6 8.0 1.0
O2 X:CAC390 1.7 10.3 1.0
C1 X:CAC390 1.9 8.8 1.0
C2 X:CAC390 1.9 10.1 1.0
ZN X:ZN400 3.3 6.7 1.0
OE2 X:GLU225 3.6 9.7 1.0
O X:HOH641 3.6 18.8 1.0
OD2 X:ASP269 3.7 9.2 1.0
O X:HOH492 3.8 16.7 1.0
OE1 X:GLU225 3.8 9.0 1.0
CD X:GLU225 4.0 8.1 1.0
OD1 X:ASP186 4.0 6.7 1.0
OE2 X:GLU226 4.1 7.2 1.0
NE1 X:TRP350 4.3 8.4 1.0
OE1 X:GLU226 4.5 7.9 1.0
OD1 X:ASP269 4.5 7.9 1.0
CD X:GLU226 4.5 6.7 1.0
CG X:ASP269 4.5 7.4 1.0
OD2 X:ASP186 4.5 6.8 1.0
NE2 X:HIS351 4.6 6.8 1.0
CG X:ASP186 4.6 6.3 1.0
CD2 X:LEU270 4.6 7.8 1.0
OD1 X:ASP326 4.8 8.3 1.0
CE1 X:HIS351 4.9 7.8 1.0
CZ2 X:TRP350 5.0 10.3 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: Tue Oct 27 16:51:31 2020

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