1cl1
From Proteopedia
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CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI
Overview
Cystathionine beta-lyase (CBL) is a member of the gamma-family of, PLP-dependent enzymes, that cleaves C beta-S bonds of a broad variety of, substrates. The crystal structure of CBL from E. coli has been solved, using MIR phases in combination with density modification. The structure, has been refined to an R-factor of 15.2% at 1.83 A resolution using, synchroton radiation diffraction data. The asymmetric unit of the crystal, cell (space group C222(1)) contains two monomers related by 2-fold, symmetry. A homotetramer with 222 symmetry is built up by crystallographic, and non-crystallographic symmetry. Each monomer of CBL can be described in, terms of three spatially and functionally different domains. The, N-terminal domain (residues 1 to 60) consists of three alpha-helices and, one ... [(full description)]
About this Structure
1CL1 is a [Single protein] structure of sequence from [Escherichia coli] with BCT as [ligand]. Active as [[1]], with EC number [4.4.1.8]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A., Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A, J Mol Biol. 1996 Sep 20;262(2):202-24. PMID:8831789
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