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Atomistry » Tungsten » PDB 1aor-2hcm » 1mu7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Tungsten » PDB 1aor-2hcm » 1mu7 » |
Tungsten in PDB 1mu7: Crystal Structure of A Human Tyrosyl-Dna Phosphodiesterase (TDP1)- Tungstate ComplexProtein crystallography data
The structure of Crystal Structure of A Human Tyrosyl-Dna Phosphodiesterase (TDP1)- Tungstate Complex, PDB code: 1mu7
was solved by
D.R.Davies,
H.Interthal,
J.J.Champoux,
W.G.J.Hol,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Tungsten Binding Sites:
The binding sites of Tungsten atom in the Crystal Structure of A Human Tyrosyl-Dna Phosphodiesterase (TDP1)- Tungstate Complex
(pdb code 1mu7). This binding sites where shown within
5.0 Angstroms radius around Tungsten atom.
In total 2 binding sites of Tungsten where determined in the Crystal Structure of A Human Tyrosyl-Dna Phosphodiesterase (TDP1)- Tungstate Complex, PDB code: 1mu7: Jump to Tungsten binding site number: 1; 2; Tungsten binding site 1 out of 2 in 1mu7Go back to Tungsten Binding Sites List in 1mu7
Tungsten binding site 1 out
of 2 in the Crystal Structure of A Human Tyrosyl-Dna Phosphodiesterase (TDP1)- Tungstate Complex
Mono view Stereo pair view
Tungsten binding site 2 out of 2 in 1mu7Go back to Tungsten Binding Sites List in 1mu7
Tungsten binding site 2 out
of 2 in the Crystal Structure of A Human Tyrosyl-Dna Phosphodiesterase (TDP1)- Tungstate Complex
Mono view Stereo pair view
Reference:
D.R.Davies,
H.Interthal,
J.J.Champoux,
W.G.J.Hol.
Insights Into Substrate Binding and Catalytic Mechanism of Human Tyrosyl-Dna Phosphodiesterase (TDP1) From Vanadate- and Tungstate-Inhibited Structures J.Mol.Biol. V. 324 917 2003.
Page generated: Wed Dec 16 02:33:11 2020
ISSN: ISSN 0022-2836 PubMed: 12470949 DOI: 10.1016/S0022-2836(02)01154-3 |
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