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PDBe Entry: 2gqn 
Cystathionine Beta-Lyase (CBL) from Escherichia Coli in complex with N-Hydrazinocarbonylmethyl-2-Nitro-Benzamide
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LYASE
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X-RAY DIFFRACTION
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Resolution: 1.8 Å, R-factor: 17.676%, Free R-factor: 22.691%, Spacegroup: C 2 2 21
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06/03/2007, deposition: 21/04/2006, last revision: 24/02/2009
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Summerfield, R.; Junop, M.S.
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Inhibitors of Bacterial Cystathionine beta-Lyase: Leads for New Antimicrobial Agents and Probes of Enzyme Structure and Function.
J.MED.CHEM. vol:50, pag:755-764 (2007) [PubMed ID 17300162 ]
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protein-inhibitor complex, PLP cofactor covalently bount to BLP Inhibitor, LYASE
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4.4.1.8 ExPASy BRENDA (A B)
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Escherichia coli 562(A B)
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Cystathionine beta-lyase (EC 4.4.1.8) (CBL) (Beta-cystathionase) (Cysteine lyase) P06721 (A B)
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A, B
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2fq6
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| A, B |
Cystathionine beta-lyase |
Protein |
P06721 (METC_ECOLI)
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415 |
94% |
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| A, B |
(5-HYDROXY-6-METHYL-4-((2-(2-(2-NITROBENZAMIDO)ACETYL)HYDRAZINYL)METHYL)PYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE |
BLP
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