Structure of PDB 5x8f Chain D

Receptor sequence
>5x8fD (length=484) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
LTEQPNWLMQRAQLTPERIALIYEDQTVTFAELFAASKRMAEQLAAHSVR
KGDTAAILLQNRAEMVYAVHACFLLGVKAVLLNTKLSTHERLFQLEDSGS
GFLLTDSSFEKKEYEHIVQTIDVDELMKEAAEEIEIEAYMQMDATATLMY
TSGTTGKPKGVQQTFGNHYFSAVSSALNLGITEQDRWLIALPLFHISGLS
ALFKSVIYGMTVVLHQRFSVSDVLHSINRHEVTMISAVQTMLASLLEETN
RCPESIRCILLGGGPAPLPLLEECREKGFPVFQSYGMTETCSQIVTLSPE
FSMEKLGSAGKPLFSCEIKIERDGQVCEPYEHGEIMVKGPNVMKSYFNRE
SANEASFQNGWLKTGDLGYLDNEGFLYVLDRRSDLIISGGENIYPAEVES
VLLSHPAVAEAGVSGAEDKKWGKVPHAYLVLHKPVSAGELTDYCKERLAK
YKRPKKFFVLDRLPRNASNKLLRNQLKDARKGEL
3D structure
PDB5x8f Crystal structure of the thioesterification conformation of Bacillus subtilis o-succinylbenzoyl-CoA synthetase reveals a distinct substrate-binding mode
ChainD
Resolution1.763 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T152 S172 H196 T289 E290 I388 N393 K471
Catalytic site (residue number reindexed from 1) T151 S171 H195 T288 E289 I387 N392 K470
Enzyme Commision number 6.2.1.26: o-succinylbenzoate--CoA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008756 o-succinylbenzoate-CoA ligase activity
GO:0016405 CoA-ligase activity
GO:0016874 ligase activity
Biological Process
GO:0009234 menaquinone biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5x8f, PDBe:5x8f, PDBj:5x8f
PDBsum5x8f
PubMed28559280
UniProtP23971|MENE_BACSU 2-succinylbenzoate--CoA ligase (Gene Name=menE)

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