Structure of PDB 1fhv Chain A

Receptor sequence
>1fhvA (length=322) Species: 562 (Escherichia coli) [Search protein sequence]
GSAMRSAQVYRWQIPMDAGVVLRDRRLKTRDGLYVCLREGREGWGEISPL
PGFSQETWEEAQSVLLAWVNNWLAGDCELPQMPSVAFGVSCALAELTDTL
PQAANYRAAPLCNGDPDDLILKLADMPGEKVAKVKVGLYEAVRDGMVVNL
LLEAIPDLHLRLDANRAWTPLKGQQFAKYVNPDYRDRIAFLEEPCKTRDD
SRAFARETGIAIAWDESLREPDFAFVAEEGVRAVVIKPTLTGSLEKVREQ
VQAAHALGLTAVISSSIESSLGLTQLARIAAWLTPDTIPGLDTLDLMQAQ
QVRRWPGSTLPVVEVDALERLL
3D structure
PDB1fhv Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate.
ChainA
Resolution1.77 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K133 D161 E190 D213 K235
Catalytic site (residue number reindexed from 1) K135 D163 E192 D215 K237
Enzyme Commision number 4.2.1.113: o-succinylbenzoate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A D161 E190 D213 D163 E192 D215
BS02 OSB A K131 D161 K235 S262 S263 G288 K133 D163 K237 S264 S265 G290
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1fhv, PDBe:1fhv, PDBj:1fhv
PDBsum1fhv
PubMed10978150
UniProtP29208|MENC_ECOLI o-succinylbenzoate synthase (Gene Name=menC)

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