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Structure paper

TitleThe mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTP.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 71, Page 516-524, Year 2015
Publish dateDec 11, 2014 (structure data deposition date)
AuthorsZhu, C.F. / Wei, W. / Peng, X. / Dong, Y.H. / Gong, Y. / Yu, X.F.
External linksActa Crystallogr. ,Sect. D / PubMed:25760601
MethodsX-ray diffraction
Resolution2.1 - 2.6 Å
Structure data

PDB-4rxo:
The structure of GTP-bound SAMHD1
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4rxp:
The structure of GTP-dATP-bound SAMHD1
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4rxq:
The structure of GTP-dUTP-bound SAMHD1
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4rxr:
The structure of GTP-dCTP-bound SAMHD1
Method: X-RAY DIFFRACTION / Resolution: 2.117 Å

PDB-4rxs:
The structure of GTP-dTTP-bound SAMHD1
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-DTP:
2'-DEOXYADENOSINE 5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-DUT:
DEOXYURIDINE-5'-TRIPHOSPHATE

ChemComp-DCP:
2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE

ChemComp-TTP:
THYMIDINE-5'-TRIPHOSPHATE

Source
  • homo sapiens (human)
KeywordsHYDROLASE / HD-domain / dNTP and GTP binding / phosphorylation

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