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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:

Resolution Low / High (Å) 29.820 / 2.65
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 102.021, 102.021, 265.001, 90.00, 90.00, 120.00
R / Rfree (%) 17.35 / 22.7

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 5aja

Go back to Zinc Binding Sites List in 5aja
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

A full contact list of Zinc with other atoms in the Zn binding site number 1 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) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1086

b:0.0
occ:1.00
ND1 B:HIS35 2.3 90.4 1.0
NE2 B:HIS78 2.4 85.8 1.0
SG B:CYS83 2.5 0.7 1.0
O B:HOH2002 2.9 75.8 1.0
CE1 B:HIS35 3.1 82.8 1.0
CD2 B:HIS78 3.2 84.0 1.0
CG B:HIS35 3.3 87.3 1.0
CE1 B:HIS78 3.4 94.9 1.0
CB B:CYS83 3.6 0.8 1.0
CB B:HIS35 3.8 83.5 1.0
CA B:CYS83 4.1 0.1 1.0
CA B:HIS35 4.2 78.6 1.0
NE2 B:HIS35 4.3 87.9 1.0
CD B:PRO84 4.3 0.4 1.0
CG B:HIS78 4.4 78.5 1.0
CD2 B:HIS35 4.4 85.8 1.0
ND1 B:HIS78 4.5 91.8 1.0
O B:LEU34 4.7 84.1 1.0
N B:PRO84 4.7 0.4 1.0
C B:CYS83 4.8 0.7 1.0
O B:HIS35 5.0 87.9 1.0

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.
ISSN: ISSN 1931-3128
PubMed: 25856754
DOI: 10.1016/J.CHOM.2015.03.004
Page generated: Wed Dec 16 06:03:15 2020

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