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Structure paper

TitleCrystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor.
Journal, issue, pagesJ. Mol. Biol., Vol. 311, Page 789-801, Year 2001
Publish dateFeb 19, 2001 (structure data deposition date)
AuthorsSteegborn, C. / Laber, B. / Messerschmidt, A. / Huber, R. / Clausen, T.
External linksJ. Mol. Biol. / PubMed:11518531
MethodsX-ray diffraction
Resolution3.1 - 3.25 Å
Structure data

PDB-1i41:
CYSTATHIONINE GAMMA-SYNTHASE IN COMPLEX WITH THE INHIBITOR APPA
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-1i43:
CYSTATHIONINE GAMMA-SYNTHASE IN COMPLEX WITH THE INHIBITOR PPCA
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-1i48:
CYSTATHIONINE GAMMA-SYNTHASE IN COMPLEX WITH THE INHIBITOR CTCPO
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

Chemicals

ChemComp-HEN:
2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-IMINO]-5-PHOSPHONO-PENT-3-ENOIC ACID

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-PMC:
3-(PHOSPHONOMETHYL)PYRIDINE-2-CARBOXYLIC ACID

ChemComp-CCO:
CARBOXYMETHYLTHIO-3-(3-CHLOROPHENYL)-1,2,4-OXADIAZOL

Source
  • nicotiana tabacum (common tobacco)
KeywordsLYASE / PLP-dependent enzyme / homotetramer / inhibitor complex / APPA / PPCA / CTCPO

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