Structure of PDB 2qvh Chain B

Receptor sequence
>2qvhB (length=311) Species: 269800 (Thermobifida fusca YX) [Search protein sequence]
SLTGRAFAIPLRTRFRGITVREGMLVRGAAGWGEFSPFAEYGPRECARWW
AACYEAAELGWPAPVRDTVPVNATVPAVGPEEAARIVASSGCTTAKVKVA
ERGQSEANDVARVEAVRDALGPRGRVRIDVNGAWDVDTAVRMIRLLDRFE
LEYVEQPCATVDELAEVRRRVSVPIAADESIRRAEDPLRVRDAEAADVVV
LKVQPLGGVRAALRLAEECGLPVVVSSAVETSVGLAAGVALAAALPELPY
ACGLATLRLLHADVCDDPLLPVHGVLPVRRVDVSEQRLAEVEIDPAAWQA
RLAAARAAWEQ
3D structure
PDB2qvh Crystal structure of O-succinylbenzoate synthase complexed with O-succinyl benzoate.
ChainB
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T75 K97 K99 D130 E156 D179 E180 V200 K203 S228 A229 G254
Catalytic site (residue number reindexed from 1) T74 K96 K98 D129 E155 D178 E179 V199 K202 S227 A228 G253
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 B D130 E156 D179 D129 E155 D178
BS02 OSB B T75 K97 D130 D179 K203 S227 S228 V230 G254 T74 K96 D129 D178 K202 S226 S227 V229 G253
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:0009063 amino acid catabolic process
GO:0009234 menaquinone biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qvh, PDBe:2qvh, PDBj:2qvh
PDBsum2qvh
PubMed
UniProtQ47Q21|MENC_THEFY o-succinylbenzoate synthase (Gene Name=menC)

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