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Zinc in PDB 5wri: Crystal Structure of Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide

Enzymatic activity of Crystal Structure of Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide

All present enzymatic activity of Crystal Structure of Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide:
2.8.2.20;

Protein crystallography data

The structure of Crystal Structure of Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide, PDB code: 5wri was solved by S.Tanaka, T.Nishiyori, H.Kojo, R.Otsubo, Y.Kakuta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.34 / 1.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.576, 155.972, 48.892, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 17.8

Other elements in 5wri:

The structure of Crystal Structure of Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide (pdb code 5wri). 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 Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide, PDB code: 5wri:

Zinc binding site 1 out of 1 in 5wri

Go back to Zinc Binding Sites List in 5wri
Zinc binding site 1 out of 1 in the Crystal Structure of Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide


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 Human Tyrosylprotein Sulfotransferase-1 Complexed with Pap and C4 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn403

b:20.8
occ:1.00
 OE1 B:GLU269 1.9 22.1 1.0
ND1 B:HIS267 2.2 17.3 1.0
CD B:GLU269 3.0 20.2 1.0
CE1 B:HIS267 3.0 17.7 1.0
OE2 B:GLU270 3.1 27.9 0.7
CG B:HIS267 3.3 16.2 1.0
OE2 B:GLU269 3.4 17.7 1.0
O B:HOH593 3.6 34.6 1.0
CB B:HIS267 3.7 15.0 1.0
CD B:GLU270 4.2 24.8 0.7
CA B:HIS267 4.2 14.3 1.0
NE2 B:HIS267 4.2 20.9 1.0
CG B:GLU269 4.2 20.2 1.0
CD2 B:HIS267 4.3 17.8 1.0
CG B:GLU270 4.5 26.7 1.0
O B:LEU266 4.8 17.2 1.0
O B:HOH709 4.8 50.4 1.0
O B:HOH657 4.9 17.9 1.0

Reference:

S.Tanaka, T.Nishiyori, H.Kojo, R.Otsubo, M.Tsuruta, K.Kurogi, M.C.Liu, M.Suiko, Y.Sakakibara, Y.Kakuta. Structural Basis For the Broad Substrate Specificity of the Human Tyrosylprotein Sulfotransferase-1. Sci Rep V. 7 8776 2017.
ISSN: ESSN 2045-2322
PubMed: 28821720
DOI: 10.1038/S41598-017-07141-8
Page generated: Mon Oct 28 14:37:47 2024

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