Structure of PDB 5x8g Chain B Binding Site BS02

Receptor Information
>5x8g Chain B (length=482) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TEQPNWLMQRAQLTPERIALIYEDQTVTFAELFAASKRMAEQLAAHSVRK
GDTAAILLQNRAEMVYAVHACFLLGVKAVLLNTKLSTHERLFQLEDSGSG
FLLTDSSFEKKEYEHIVQTIDVDELMKEAAEEIEIEAYMQMDATATLMYT
SGTTGKPKGVQQTFGNHYFSAVSSALNLGITEQDRWLIALPLFHISGLSA
LFKSVIYGMTVVLHQRFSVSDVLHSINRHEVTMISAVQTMLASLLEETNR
CPESIRCILLGGGPAPLPLLEECREKGFPVFQSYGMTETCSQIVTLSPEF
SMEKLGSAGKPLFSCEIKIEGQVCEPYEHGEIMVKGPNVMKSYFNRESAN
EASFQNGWLKTGDLGYLDNEGFLYVLDRRSDLIISGGENIYPAEVESVLL
SHPAVAEAGVSGAEDKKWGKVPHAYLVLHKPVSAGELTDYCKERLAKYKR
PKKFFVLDRLPRNASNKLLRNQLKDARKGELL
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain5x8g Chain B Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5x8g Crystal structure of the thioesterification conformation of Bacillus subtilis o-succinylbenzoyl-CoA synthetase reveals a distinct substrate-binding mode
Resolution1.9 Å
Binding residue
(original residue number in PDB)		H196 I197 T289
Binding residue
(residue number reindexed from 1)		H194 I195 T287
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T152 S172 H196 T289 E290 I388 N393 K471
Catalytic site (residue number reindexed from 1) T150 S170 H194 T287 E288 I384 N389 K467
Enzyme Commision number 6.2.1.26: o-succinylbenzoate--CoA ligase.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5x8g, PDBe:5x8g, PDBj:5x8g
PDBsum5x8g
PubMed28559280
UniProtP23971|MENE_BACSU 2-succinylbenzoate--CoA ligase (Gene Name=menE)

[Back to BioLiP]