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Zinc in PDB 3si2: Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150)

Enzymatic activity of Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150)

All present enzymatic activity of Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150):
2.3.2.5;

Protein crystallography data

The structure of Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150), PDB code: 3si2 was solved by C.Parthier, D.Carrillo, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.05 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.760, 83.060, 95.710, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 26

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150) (pdb code 3si2). 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 Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150), PDB code: 3si2:

Zinc binding site 1 out of 1 in 3si2

Go back to Zinc Binding Sites List in 3si2
Zinc binding site 1 out of 1 in the Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Glycosylated Murine Glutaminyl Cyclase in Presence of the Inhibitor PQ50 (PDBD150) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:12.0
occ:1.00
OE2 A:GLU203 1.8 12.2 1.0
OD2 A:ASP160 1.9 11.4 1.0
NAM A:PBD999 2.0 14.6 1.0
NE2 A:HIS331 2.1 9.6 1.0
CD A:GLU203 2.7 13.0 1.0
CG A:ASP160 2.7 11.4 1.0
OD1 A:ASP160 2.8 7.9 1.0
OE1 A:GLU203 2.9 11.7 1.0
CD2 A:HIS331 2.9 13.2 1.0
CAH A:PBD999 2.9 14.1 1.0
CAD A:PBD999 3.0 15.2 1.0
CE1 A:HIS331 3.1 14.4 1.0
NE1 A:TRP330 3.8 11.9 1.0
O A:HOH409 3.9 13.7 1.0
NAV A:PBD999 4.1 14.2 1.0
CG A:HIS331 4.1 15.6 1.0
CG A:GLU203 4.1 11.3 1.0
CB A:ASP160 4.1 11.4 1.0
CAG A:PBD999 4.1 14.2 1.0
ND1 A:HIS331 4.2 12.5 1.0
CE2 A:TRP330 4.4 14.5 1.0
OE1 A:GLU202 4.5 14.6 1.0
O A:HOH517 4.5 13.8 1.0
CD1 A:TRP330 4.5 11.3 1.0
CE1 A:HIS141 4.6 9.2 1.0
CZ2 A:TRP330 4.6 13.6 1.0
NE2 A:HIS141 4.7 13.7 1.0
O A:ASP160 4.8 10.5 1.0
CD A:LYS145 4.9 9.6 1.0
CD2 A:LEU250 4.9 11.4 1.0
O A:HOH524 5.0 14.1 1.0
CB A:LYS145 5.0 8.9 1.0

Reference:

D.Ruiz-Carrillo, B.Koch, C.Parthier, M.Wermann, T.Dambe, M.Buchholz, H.H.Ludwig, U.Heiser, J.U.Rahfeld, M.T.Stubbs, S.Schilling, H.U.Demuth. Structures of Glycosylated Mammalian Glutaminyl Cyclases Reveal Conformational Variability Near the Active Center. Biochemistry V. 50 6280 2011.
ISSN: ISSN 0006-2960
PubMed: 21671571
DOI: 10.1021/BI200249H
Page generated: Wed Dec 16 04:50:13 2020

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