Structure of PDB 3ouz Chain B Binding Site BS02

Receptor Information
>3ouz Chain B (length=443) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MEIKSILIANRGEIALRALRTIKEMGKKAICVYSEADKDALYLKYADASI
CIGKARSSESYLNIPAIIAAAEIAEADAIFPGYGFLSENQNFVEICAKHN
IKFIGPSVEAMNLMSDKSKAKQVMQRAGVPVIPGSDGALAGAEAAKKLAK
EIGYPVILKAAAGGGGRGMRVVENEKDLEKAYWSAESEAMTAFGDGTMYM
EKYIQNPRHIEVQVIGDSFGNVIHVGERDCSMQRRHQKLIEESPAILLDE
KTRTRLHETAIKAAKAIGYEGAGTFEFLVDKNLDFYFIEMNTRLQVEHCV
SEMVSGIDIIEQMIKVAEGYALPSQESIKLNGHSIECRITAEDSKTFLPS
PGKITKYIPPAGRNVRMESHCYQDYSVPAYYDSMIGKLVVWAEDRNKAIA
KMKVALDELLISGIKTTKDFHLSMMENPDFINNNYDTNYLARH
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3ouz Chain B Residue 459 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ouz Crystal Structure of Biotin Carboxylase-ADP complex from Campylobacter jejuni
Resolution1.902 Å
Binding residue
(original residue number in PDB)		E276 E289
Binding residue
(residue number reindexed from 1)		E276 E289
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K159 G165 G166 H209 K238 T274 E276 E289 N291 V296 E297 R338
Catalytic site (residue number reindexed from 1) K159 G165 G166 H209 K238 T274 E276 E289 N291 V296 E297 R338
Enzyme Commision number 6.3.4.14: biotin carboxylase.
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0004075 biotin carboxylase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ouz, PDBe:3ouz, PDBj:3ouz
PDBsum3ouz
PubMed
UniProtQ0P8W7

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