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Zinc in PDB 1eh6: Human O6-Alkylguanine-Dna Alkyltransferase

Enzymatic activity of Human O6-Alkylguanine-Dna Alkyltransferase

All present enzymatic activity of Human O6-Alkylguanine-Dna Alkyltransferase:
2.1.1.63;

Protein crystallography data

The structure of Human O6-Alkylguanine-Dna Alkyltransferase, PDB code: 1eh6 was solved by D.S.Daniels, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.21 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.283, 71.283, 73.611, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 21.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Human O6-Alkylguanine-Dna Alkyltransferase (pdb code 1eh6). 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 Human O6-Alkylguanine-Dna Alkyltransferase, PDB code: 1eh6:

Zinc binding site 1 out of 1 in 1eh6

Go back to Zinc Binding Sites List in 1eh6
Zinc binding site 1 out of 1 in the Human O6-Alkylguanine-Dna Alkyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human O6-Alkylguanine-Dna Alkyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn208

b:41.9
occ:0.70
ND1 A:HIS85 2.0 39.0 1.0
NE2 A:HIS29 2.1 39.0 1.0
SG A:CYS24 2.3 36.9 1.0
SG A:CYS5 2.5 56.1 1.0
CD2 A:HIS29 3.0 36.5 1.0
CE1 A:HIS85 3.0 39.6 1.0
CG A:HIS85 3.1 38.0 1.0
CE1 A:HIS29 3.1 38.6 1.0
CB A:HIS85 3.5 36.0 1.0
CB A:CYS24 3.7 35.3 1.0
O A:HIS85 4.0 37.9 1.0
CB A:CYS5 4.0 60.2 1.0
NE2 A:HIS85 4.2 39.6 1.0
CG A:HIS29 4.2 34.9 1.0
CD2 A:HIS85 4.2 38.3 1.0
ND1 A:HIS29 4.2 37.0 1.0
CB A:GLN26 4.5 41.0 1.0
O A:GLY27 4.6 29.2 1.0
C A:HIS85 4.6 36.5 1.0
N A:CYS24 4.7 33.0 1.0
CA A:CYS5 4.7 60.2 1.0
CA A:HIS85 4.7 35.3 1.0
CA A:CYS24 4.8 35.1 1.0
CE A:MET7 4.8 52.9 1.0
OE1 A:GLN26 4.9 48.5 1.0
N A:GLY27 5.0 34.4 1.0

Reference:

D.S.Daniels, C.D.Mol, A.S.Arvai, S.Kanugula, A.E.Pegg, J.A.Tainer. Active and Alkylated Human Agt Structures: A Novel Zinc Site, Inhibitor and Extrahelical Base Binding. Embo J. V. 19 1719 2000.
ISSN: ISSN 0261-4189
PubMed: 10747039
DOI: 10.1093/EMBOJ/19.7.1719
Page generated: Wed Dec 16 02:48:18 2020

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