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EBI PDBe PDBeView

PDBe Entry: 1cl2 view

CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI IN COMPLEX WITH AMINOETHOXYVINYLGLYCINE
Summary
Header METHIONINE BIOSYNTHESISsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 16.4%, Spacegroup: C 2 2 21
Released 09/09/1998, deposition: 04/09/1997, last revision: 24/02/2009
Authors Clausen, T.search; Huber, R.search; Messerschmidt, A.search
Primary citation Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study.
BIOCHEMISTRYsearch vol:36, pag:12633-12643 (1997) [PubMed ID 9376370 ]search
Keywords METHIONINE BIOSYNTHESISsearch, PLP-DEPENDENT ENZYMESsearch, C-S BETA LYASEsearch, AMINOETHOXYVINYLGLYCINEsearch, SLOW-BINDING INHIBITIONsearch
EC 4.4.1.8 ExPASy BRENDA search (A B)
Organism Escherichia coli K-12 83333search(A B)
UniProt Cystathionine beta-lyase (EC 4.4.1.8) (CBL) (Beta-cystathionase) (Cysteine lyase) P06721search (A B)
Solvent A, B
Polymers
Id Name Type UniProt Residues Observed
A, B CYSTATHIONINE BETA-LYASE Protein P06721 (METC_ECOLI)search
 395 99%
Heterogens
Id Name Ligands
A, B 4-(2-AMINO-ETHOXY)-2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-BUT-3-ENOIC ACID PPG search
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