Structure of PDB 3h7v Chain A

Receptor sequence
>3h7vA (length=320) Species: 197221 (Thermosynechococcus vestitus BP-1) [Search protein sequence]
LRWQWRIYEEPLQEPLTTAQGVWRSRSGIYLRLEDEQGQVGYGEIAPLPG
WGSETLNADIALCQQLPGHLTPEIMATIPEALPAAQFGFATAWQSVGRLP
YRVRPWPICALLGSGQAALEQWQQSWQRGQTTFKWKVGVMSPEEEQAILK
ALLAALPPGAKLRLDANGSWDRATANRWFAWLDRHGNGKIEYVEQPLPPD
QWQALLSLAQTVTTAIALDESVVSAAEVQRWVDRGWPGFFVIKTALFGDP
DSLSLLLRRGLEPQRLVFSSALEGAIARTAIFHLLETWQPCHALGFGVDR
WRSAPLLTTLTAYERLWERL
3D structure
PDB3h7v Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K134 K136 D165 E194 D219 K243
Catalytic site (residue number reindexed from 1) K134 K136 D165 E194 D219 K243
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 D165 E194 D219 D165 E194 D219
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
GO:0042372 phylloquinone biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3h7v, PDBe:3h7v, PDBj:3h7v
PDBsum3h7v
PubMed24872444
UniProtQ8DJP8|MENC_THEVB o-succinylbenzoate synthase (Gene Name=menC)

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