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Structure paper

TitleMechanism and substrate recognition of human holo ACP synthase.
Journal, issue, pagesChem. Biol., Vol. 14, Page 1243-1253, Year 2007
Publish dateJul 29, 2005 (structure data deposition date)
AuthorsBunkoczi, G. / Pasta, S. / Joshi, A. / Wu, X. / Kavanagh, K.L. / Smith, S. / Oppermann, U.
External linksChem. Biol. / PubMed:18022563
MethodsX-ray diffraction
Resolution1.93 - 2.7 Å
Structure data

PDB-2byd:
Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2c43:
STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE- PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

PDB-2cg5:
Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in complex with cytosolic acyl carrier protein and coenzyme A
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-BR:
BROMIDE ION

ChemComp-HOH:
WATER

ChemComp-COA:
COENZYME A

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-NI:
NICKEL (II) ION

ChemComp-PO4:
PHOSPHATE ION

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / FATTY ACID BIOSYNTHESIS / PHOSPHOPANTETHEINE TRANSFERASE / COENZYME A / TRANSFERASE/HYDROLASE / TRANSFERASE-HYDROLASE COMPLEX / TRANSFERASE-HYDROLASE (COMPLEX) / FASN / ACP / HYDROLASE / LIPID SYNTHESIS / LYASE / COMPLEX

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