1cl1 Summary

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CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI

The structure was published by Clausen, T., Huber, R., Laber, B., Pohlenz, H.D., and Messerschmidt, A., in 1996 in a paper entitled "Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.83 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of CYSTATHIONINE BETA-LYASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CYSTATHIONINE BETA-LYASE P06721 (1-395) (METC_ECOLI)search Escherichia coli K-12search 100% 395 99%
B CYSTATHIONINE BETA-LYASE P06721 (1-395) (METC_ECOLI)search Escherichia coli K-12search 100% 395 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P06721 (1 - 395) CYSTATHIONINE BETA-LYASE Escherichia coli K-12

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P06721) Cystathionine synthase-likesearch Type I PLP-dependent aspartate aminotransferase-like (Major domain)search, Aspartate Aminotransferase, domain 1search PF01053: Cys/Met metabolism PLP-dependent enzymesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P06721) cellular amino acid metabolic processsearch cellular amino acid biosynthetic processsearch methionine biosynthetic processsearch catalytic activitysearch pyridoxal phosphate bindingsearch cystathionine beta-lyase activitysearch L-cysteine desulfhydrase activitysearch lyase activitysearch cytoplasmsearch

Chain InterPro annotation
A, B Cys/Met metabolism, pyridoxal phosphate-dependent enzymesearch Cystathionine beta-lyase, bacterialsearch Pyridoxal phosphate-dependent transferase, major region, subdomain 1search Pyridoxal phosphate-dependent transferase, major region, subdomain 2search Pyridoxal phosphate-dependent transferasesearch