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Structure paper

TitleMultisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1
Journal, issue, pagesJ. Mol. Biol., Vol. 363, Page 201-214, Year 2006
Publish dateJun 2, 2006 (structure data deposition date)
AuthorsBencharit, S. / Edwards, C.C. / Morton, C.L. / Howard-Williams, E.L. / Kuhn, P. / Potter, P.M. / Redinbo, M.R.
External linksJ. Mol. Biol. / PubMed:16962139
MethodsX-ray diffraction
Resolution2 - 3.2 Å
Structure data

PDB-2dqy:
Crystal structure of human carboxylesterase in complex with cholate and palmitate
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-2dqz:
Crystal structure of human carboxylesterase in complex with homatropine, coenzyme A, and palmitate
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-2dr0:
Crystal structure of human carboxylesterase in complex with taurocholate
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-2h7c:
Crystal structure of human carboxylesterase in complex with Coenzyme A
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-SIA:
N-acetyl-alpha-neuraminic acid

ChemComp-SO4:
SULFATE ION

ChemComp-CHD:
CHOLIC ACID

ChemComp-PLM:
PALMITIC ACID

ChemComp-HOH:
WATER

ChemComp-F:
FLUORIDE ION

ChemComp-HTQ:
HOMOTROPINE

ChemComp-COA:
COENZYME A

ChemComp-TCH:
TAUROCHOLIC ACID

Source
  • homo sapiens (human)
KeywordsHYDROLASE / cholesterol metabolism / foam cells / macrophage / monocyte / atherosclerosis / cholesterol / esterase / liver / enzyme / cholesteryl esterase

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