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Structure paper

TitleInhibitors of bacterial cystathionine beta-lyase: leads for new antimicrobial agents and probes of enzyme structure and function.
Journal, issue, pagesJ. Med. Chem., Vol. 50, Page 755-764, Year 2007
Publish dateJan 17, 2006 (structure data deposition date)
AuthorsEjim, L.J. / Blanchard, J.E. / Koteva, K.P. / Sumerfield, R. / Elowe, N.H. / Chechetto, J.D. / Brown, E.D. / Junop, M.S. / Wright, G.D.
External linksJ. Med. Chem. / PubMed:17300162
MethodsX-ray diffraction
Resolution1.78 - 1.8 Å
Structure data

PDB-2fq6:
Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

PDB-2gqn:
Cystathionine Beta-Lyase (CBL) from Escherichia Coli in complex with N-Hydrazinocarbonylmethyl-2-Nitro-Benzamide
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-P3F:
PHOSPHORIC ACID MONO-(5-HYDROXY-6-METHYL-4-{[2-(2-TRIFLUOROMETHYL-BENZOYLAMINO)-ACETYL]-HYDRAZONOMETHYL}-PYRIDIN-3-YLMETHYL)ESTER

ChemComp-HOH:
WATER

ChemComp-BLP:
(5-HYDROXY-6-METHYL-4-((2-(2-(2-NITROBENZAMIDO)ACETYL)HYDRAZINYL)METHYL)PYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE

Source
  • escherichia coli (E. coli)
KeywordsLYASE / PROTEIN-INHIBITOR COMPLEX / PLP COFACTOR COVALENTLY BOUND TO P3F INHIBITOR / PLP cofactor covalently bount to BLP Inhibitor

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