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Structure paper

TitlePost-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and release.
Journal, issue, pagesBiochemistry, Vol. 50, Page 2870-2880, Year 2011
Publish dateJan 20, 2011 (structure data deposition date)
AuthorsHazra, S. / Szewczak, A. / Ort, S. / Konrad, M. / Lavie, A.
External linksBiochemistry / PubMed:21351740
MethodsX-ray diffraction
Resolution1.897 - 2.49 Å
Structure data

PDB-3qej:
S74E-dCK mutant in complex with UDP
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

PDB-3qen:
S74E dCK in complex with 5-bromodeoxycytidine and UDP
Method: X-RAY DIFFRACTION / Resolution: 1.997 Å

PDB-3qeo:
S74E-R104M-D133A dCK variant in complex with L-deoxythymidine and UDP
Method: X-RAY DIFFRACTION / Resolution: 1.897 Å

Chemicals

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM

ChemComp-HOH:
WATER

ChemComp-5BT:
5-bromo-2'-deoxycytidine

ChemComp-LLT:
L-deoxythymidine / antivirus*YM

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / alpha/beta / phosphoryl transfer / ATP binding / phosphorylation

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