Structure of PDB 1r6w Chain A Binding Site BS02

Receptor Information
>1r6w Chain A (length=321) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SHMRSAQVYRWQIPMDAGVVLDRRLKTRDGLYVCLREGEREGWGEISPLP
GFSQETWEEAQSVLLAWVNNWLAGDCELPQMPSVAFGVSCALAELTDTLP
QAANYRAAPLCNGDPDDLILKLADMPGEKVAKVRVGLYEAVRDGMVVNLL
LEAIPDLHLRLDANRAWTPLKGQQFAKYVNPDYRDRIAFLEEPCKTRDDS
RAFARETGIAIAWDESLREPDFAFVAEEGVRAVVIKPTLTGSLEKVREQV
QAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQQ
VRRWPGSTLPVVEVDALERLL
Ligand information
Ligand ID164
InChIInChI=1S/C11H12O6/c12-7(4-5-9(14)15)6-2-1-3-8(13)10(6)11(16)17/h1-3,8,10,13H,4-5H2,(H,14,15)(H,16,17)/t8-,10-/m1/s1
InChIKeyQJYRAJSESKVEAE-PSASIEDQSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(C1=CC=CC(O)C1C(=O)O)CCC(=O)O
OpenEye OEToolkits 1.5.0C1=C[C@H]([C@@H](C(=C1)C(=O)CCC(=O)O)C(=O)O)O
OpenEye OEToolkits 1.5.0C1=CC(C(C(=C1)C(=O)CCC(=O)O)C(=O)O)O
CACTVS 3.341O[CH]1C=CC=C([CH]1C(O)=O)C(=O)CCC(O)=O
CACTVS 3.341O[C@@H]1C=CC=C([C@H]1C(O)=O)C(=O)CCC(O)=O
FormulaC11 H12 O6
Name2-(3-CARBOXYPROPIONYL)-6-HYDROXY-CYCLOHEXA-2,4-DIENE CARBOXYLIC ACID
ChEMBL
DrugBankDB06864
ZINCZINC000004096915
PDB chain1r6w Chain A Residue 735 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1r6w Evolution of Enzymatic Activity in the Enolase Superfamily: Structural and Mutagenic Studies of the Mechanism of the Reaction Catalyzed by o-Succinylbenzoate Synthase from Escherichia coli
Resolution1.62 Å
Binding residue
(original residue number in PDB)		F51 K131 D161 D213 K235 S262 G288
Binding residue
(residue number reindexed from 1)		F52 K132 D162 D214 K236 S263 G289
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R133 D161 E190 D213 K235
Catalytic site (residue number reindexed from 1) R134 D162 E191 D214 K236
Enzyme Commision number 4.2.1.113: o-succinylbenzoate synthase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0043748 O-succinylbenzoate synthase activity
GO:0046872 metal ion binding
Biological Process
GO:0009234 menaquinone biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1r6w, PDBe:1r6w, PDBj:1r6w
PDBsum1r6w
PubMed14661953
UniProtP29208|MENC_ECOLI o-succinylbenzoate synthase (Gene Name=menC)

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