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Structure paper

TitleStructure and Functional Characterization of Human Aspartate Transcarbamoylase, the Target of the Anti-Tumoral Drug Pala.
Journal, issue, pagesStructure, Vol. 24, Page 1081-, Year 2016
Publish dateMar 29, 2016 (structure data deposition date)
AuthorsRuiz-Ramos, A. / Velazquez-Campoy, A. / Grande-Garcia, A. / Moreno-Morcillo, M. / Ramon-Maiques, S.
External linksStructure / PubMed:27265852
MethodsX-ray diffraction
Resolution2.1 - 3.19 Å
Structure data

PDB-5g1n:
Aspartate transcarbamoylase domain of human CAD bound to PALA
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-5g1o:
Aspartate transcarbamoylase domain of human CAD in apo form
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-5g1p:
Aspartate transcarbamoylase domain of human CAD bound to carbamoyl phosphate
Method: X-RAY DIFFRACTION / Resolution: 3.19 Å

Chemicals

ChemComp-PAL:
N-(PHOSPHONACETYL)-L-ASPARTIC ACID

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-CP:
PHOSPHORIC ACID MONO(FORMAMIDE)ESTER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / DE NOVO PYRIMIDINE SYNTHESIS / TRANSCARBAMOYLASE / TRANSCARBAMYLASE / CAD / CARBAMOYL PHOSPHATE SYNTHETASE / DIHYDROOROTASE / COOPERATIVITY

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