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Atomistry » Zinc » PDB 5af0-5amk » 5aja » |
Zinc in PDB 5aja: Crystal Structure of Mandrill SAMHD1 (Amino Acid Residues 1-114) Bound to Vpx Isolated From Mandrill and Human DCAF1 (Amino Acid Residues 1058-1396)Enzymatic activity of Crystal Structure of Mandrill SAMHD1 (Amino Acid Residues 1-114) Bound to Vpx Isolated From Mandrill and Human DCAF1 (Amino Acid Residues 1058-1396)
All present enzymatic activity of Crystal Structure of Mandrill SAMHD1 (Amino Acid Residues 1-114) Bound to Vpx Isolated From Mandrill and Human DCAF1 (Amino Acid Residues 1058-1396):
2.7.11.1; Protein crystallography data
The structure of Crystal Structure of Mandrill SAMHD1 (Amino Acid Residues 1-114) Bound to Vpx Isolated From Mandrill and Human DCAF1 (Amino Acid Residues 1058-1396), PDB code: 5aja
was solved by
D.Schwefel,
V.C.Boucherit,
E.Christodoulou,
P.A.Walker,
J.P.Stoye,
K.N.Bishop,
I.A.Taylor,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Mandrill SAMHD1 (Amino Acid Residues 1-114) Bound to Vpx Isolated From Mandrill and Human DCAF1 (Amino Acid Residues 1058-1396)
(pdb code 5aja). 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 Crystal Structure of Mandrill SAMHD1 (Amino Acid Residues 1-114) Bound to Vpx Isolated From Mandrill and Human DCAF1 (Amino Acid Residues 1058-1396), PDB code: 5aja: Zinc binding site 1 out of 1 in 5ajaGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of Mandrill SAMHD1 (Amino Acid Residues 1-114) Bound to Vpx Isolated From Mandrill and Human DCAF1 (Amino Acid Residues 1058-1396)
![]() Mono view ![]() Stereo pair view
Reference:
D.Schwefel,
V.C.Boucherit,
E.Christodoulou,
P.A.Walker,
J.P.Stoye,
K.N.Bishop,
I.A.Taylor.
Molecular Determinants For Recognition of Divergent SAMHD1 Proteins By the Lentiviral Accessory Protein Vpx. Cell Host Microbe. V. 17 489 2015.
Page generated: Sun Oct 27 13:02:13 2024
ISSN: ISSN 1931-3128 PubMed: 25856754 DOI: 10.1016/J.CHOM.2015.03.004 |
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