Structure of PDB 1cl1 Chain B Binding Site BS01

Receptor Information
>1cl1 Chain B (length=392) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGE
LFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDH
VLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFL
ESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDV
SIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITS
RGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRD
FTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPE
HIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV
Ligand information
Ligand IDBCT
InChIInChI=1S/CH2O3/c2-1(3)4/h(H2,2,3,4)/p-1
InChIKeyBVKZGUZCCUSVTD-UHFFFAOYSA-M
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(=O)(O)[O-]
CACTVS 3.341OC([O-])=O
ACDLabs 10.04[O-]C(=O)O
FormulaC H O3
NameBICARBONATE ION
ChEMBL
DrugBank
ZINC
PDB chain1cl1 Chain B Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1cl1 Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A.
Resolution1.83 Å
Binding residue
(original residue number in PDB)		Y111 X210 S339 W340 R372
Binding residue
(residue number reindexed from 1)		Y108 X207 S336 W337 R369
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R58 Y111 D185 K210
Catalytic site (residue number reindexed from 1) R55 Y108 D182 K207
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1cl1, PDBe:1cl1, PDBj:1cl1
PDBsum1cl1
PubMed8831789
UniProtP06721|METC_ECOLI Cystathionine beta-lyase MetC (Gene Name=metC)

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