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Gold in PDB 2aaq: Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi

Enzymatic activity of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi

All present enzymatic activity of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi:
1.8.1.7;

Protein crystallography data

The structure of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi, PDB code: 2aaq was solved by S.Urig, K.Fritz-Wolf, R.Reau, C.Herold-Mende, K.Toth, E.Davioud-Charvet, K.Becker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.98 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.310, 62.720, 83.990, 90.00, 122.47, 90.00
R / Rfree (%) 20.1 / 25.9

Other elements in 2aaq:

The structure of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi also contains other interesting chemical elements:

Potassium (K) 1 atom
Chlorine (Cl) 1 atom

Gold Binding Sites:

The binding sites of Gold atom in the Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi (pdb code 2aaq). This binding sites where shown within 5.0 Angstroms radius around Gold atom.
In total 2 binding sites of Gold where determined in the Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi, PDB code: 2aaq:
Jump to Gold binding site number: 1; 2;

Gold binding site 1 out of 2 in 2aaq

Go back to Gold Binding Sites List in 2aaq
Gold binding site 1 out of 2 in the Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 1 of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Au602

b:47.4
occ:1.00
P A:AUP601 2.3 50.7 1.0
CB A:CYS284 2.3 35.4 1.0
SG A:CYS284 2.4 39.5 1.0
C28 A:AUP601 3.3 52.2 1.0
C9 A:AUP601 3.3 50.4 1.0
O A:HOH912 3.4 23.8 1.0
C7 A:AUP601 3.5 52.2 1.0
C27 A:AUP601 3.6 51.8 1.0
C37 A:AUP601 3.7 53.9 1.0
C18 A:AUP601 3.7 49.8 1.0
CD1 A:ILE175 3.8 30.8 1.0
CA A:CYS284 3.8 34.6 1.0
C19 A:AUP601 3.8 50.6 1.0
O A:ASP283 4.0 34.5 1.0
C36 A:AUP601 4.1 54.0 1.0
CD2 A:LEU183 4.1 20.8 1.0
CG1 A:ILE175 4.1 31.9 1.0
C2 A:AUP601 4.2 51.4 1.0
C1 A:AUP601 4.3 51.8 1.0
CG2 A:ILE175 4.4 33.8 1.0
C A:CYS284 4.5 32.4 1.0
C29 A:AUP601 4.6 53.9 1.0
N A:CYS284 4.8 33.4 1.0
N A:LEU285 4.8 31.2 1.0
C A:ASP283 4.8 33.2 1.0
CB A:ILE175 4.9 31.9 1.0
C38 A:AUP601 5.0 54.7 1.0

Gold binding site 2 out of 2 in 2aaq

Go back to Gold Binding Sites List in 2aaq
Gold binding site 2 out of 2 in the Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 2 of Crystal Structure Analysis of the Human Glutahione Reductase, Complexed with Gopi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Au603

b:46.9
occ:1.00
SG A:CYS58 2.3 33.3 1.0
SG A:CYS63 2.3 38.9 1.0
CB A:CYS63 2.9 34.7 1.0
CB A:CYS58 2.9 38.1 1.0
O3 A:PO4504 3.0 38.6 1.0
CA A:CYS58 3.1 40.1 1.0
O2 A:PO4504 3.2 43.0 1.0
C A:CYS58 3.4 40.5 1.0
O A:CYS58 3.4 40.7 1.0
CB A:THR339 3.6 23.2 1.0
OG1 A:THR339 3.6 26.2 1.0
P A:PO4504 3.6 37.9 1.0
O2' A:FAD499 3.7 37.8 1.0
CG2 A:THR339 3.8 22.0 1.0
K A:K701 4.0 37.9 1.0
N A:CYS63 4.0 34.3 1.0
O4 A:PO4504 4.1 39.7 1.0
CA A:CYS63 4.1 33.7 1.0
N A:VAL59 4.3 41.2 1.0
C2' A:FAD499 4.4 36.5 1.0
N A:CYS58 4.4 41.1 1.0
O4' A:FAD499 4.8 34.9 1.0
N1 A:FAD499 4.9 38.0 1.0
O1 A:PO4504 4.9 38.0 1.0
C10 A:FAD499 5.0 38.7 1.0
CA A:THR339 5.0 24.0 1.0

Reference:

S.Urig, K.Fritz-Wolf, R.Reau, C.Herold-Mende, K.Toth, E.Davioud-Charvet, K.Becker. Undressing of Phosphine Gold(I) Complexes As Irreversible Inhibitors of Human Disulfide Reductases. Angew.Chem.Int.Ed.Engl. V. 45 1881 2006.
ISSN: ISSN 1433-7851
PubMed: 16493712
DOI: 10.1002/ANIE.200502756
Page generated: Wed Jul 10 14:11:42 2024

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