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Structure of PDB 1cl1 Chain A Binding Site BS01

Receptor Information >1cl1 Chain A (length=391) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] KLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGEL FYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHV LMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLE SPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVS IQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSR GLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDF TGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEH IAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV

Ligand information Ligand ID BCT InChI InChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1 InChIKey BVKZGUZCCUSVTD-UHFFFAOYSA-M SMILES Software SMILES OpenEye OEToolkits 1.5.0 C(=O)(O)[O-] CACTVS 3.341 OC([O-])=O ACDLabs 10.04 [O-]C(=O)O Formula C H O3 Name BICARBONATE ION ChEMBL DrugBank ZINC PDB chain 1cl1 Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1cl1 Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. Resolution 1.83 Å Binding residue (original residue number in PDB) Y111 S339 W340 R372 Binding residue (residue number reindexed from 1) Y107 S335 W336 R368 Annotation score 1

Enzymatic activity Catalytic site (original residue number in PDB) R58 Y111 D185 K210 Catalytic site (residue number reindexed from 1) R54 Y107 D181 K206 Enzyme Commision number 4.4.1.13: cysteine-S-conjugate beta-lyase. 4.4.1.28: L-cysteine desulfidase.

Gene Ontology Molecular Function GO:0003824 catalytic activity GO:0008784 alanine racemase activity GO:0016829 lyase activity GO:0030170 pyridoxal phosphate binding GO:0042802 identical protein binding GO:0047804 cysteine-S-conjugate beta-lyase activity GO:0080146 L-cysteine desulfhydrase activity

	Biological Process
GO:0006520	amino acid metabolic process
GO:0009086	methionine biosynthetic process
GO:0019346	transsulfuration
GO:0019450	L-cysteine catabolic process to pyruvate
GO:0051289	protein homotetramerization

	Cellular Component
GO:0005737	cytoplasm
GO:0032991	protein-containing complex

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