Structure of PDB 6eqo Chain B

Receptor sequence
>6eqoB (length=1803) Species: 237727 (Erythrobacter sp. NAP1) [Search protein sequence]
ISDRDHFQRLREECRSDPGEFHGRLAKREICWLIENPAWAFYDDAAETWT
GWDASSAAPITLDLPESFEPWERAFNDDDPPNWRWFEGGLTSTAFNEVDR
HVLSGHGDEAAMIFEGDRWNMASEGGRGGPVDSEVISRRKLLLESAKCAL
ALKALGLEAGDRIALNMPSIPEQIYWTEGAKRMGIVYTPVFGGFSDKTLS
DRIADAGARVVVTADGSYRNAQMVPFKPSYTDPALDNFIAVPVAMELLGQ
ALEVVAPEHAGLIRSEVAGLLDGEVTVERSDVMRGVGKALTAIASGEAAG
GAMTPRQAAQLRIAIASALVDSPPRVDAVVVVKHTAQPDLPWNEARDHWS
HDLTAAAGEELLKAARDAGFDVADEEALLALSDTEFVRAIWAGAPVLAVD
AEYPNFIIYTSGSTGKPKGVVHVHGGYASGVAATMPAAFGAEPGDVMYVV
ADPGWITGQSYQIAASLLSRVTTVITEGSPVFPHAGRFASIIERYGVNVF
KAGVTFLKSVMQNPENLKDIQRYDLSSLKVATFCAEPVSPAVQAFAMEHI
THRYINSYWATEHGGMVWTHFADADGFPLEADAHTYPLPWIMGDVWVEDA
DGSSNGPVEYERDTPWRVAEDGEKGEIVIALPYPYLTRTIWGDVENFTVE
HVGNLARVAGGWRGDEVRYADTYWRRWKGAWAYTQGDFAMRHPDGSFSLH
GRSDDVINVSGHRIGTEEIEGAILRDKALDPNSPVGNVIVIGAPHSQKGV
TPIAFVTPVEGRRLTQDDKRRLTDLVRTEKGAVAVPQDFIELSEFPETRS
GKYMRRMVRAVVEGGEVLRNPESLDELARAVDGWKRRQSLSDTQALFERY
RFFTIQYNLVAPGKRVATVTVKNPPVNALNERALDELVIIAEHLARKDDV
AAVVFTGSGTASFVAGADIRQMLEEVNSVEEAKALPDNAQLAFRTIEEMD
KPCIAAIQGVALGGGMEFALACHYRVAEPKARFGQPEINLRLLPGYGGTQ
RLPRLLADGGGETGLRDALDLILGGRAIDADAALAVGAVDALADGSDNAL
SHAHAMVREFVRSGDDSALGKAFAARKTQTQSWHEPASIDLDAVLEDEFL
QRILNQLEWAGRDKAGERALDAVRTGWTQGMTAGLECEAQRFAEAIIDPE
GGKTGIQQFMDKQSPPLPVRRDGVWEDDQHEATKTALIEAGDLLPLGAPF
YPGVTAIPPKQLAFGIARDPDTGAPRFGPPETHERELVVNTPKPGANEAL
IYLLSSEVNFNDIWALTGIPVSPFDAHDEDVQITGSGGLALVAALGSELK
EEGRLQVGDLVSVYSGTSELLSPLAGDDPMYAGFAIQGYETKTGSHAQFL
TVQGPQLHRPPADLTLEQAGAYTLNLGTVARCLFTTLEIQAGKTAFVEGS
ATGTGLDALKSSVRTGLAVTGLVSSEDRAEFVKSHGSVGAINRKDPEIAD
CFTPVPDDPDEARQWEADGEKLLDAYRETNGGKLADYVVSHAGERAFPRS
FQLLAEGGRLAFYGASSGYHFSFMGKGGEARPDEMLARANLRGGESVLLY
YGPGSHELADEKGLEMVEAARLMKARMVIVTTSDGQREFLQSLGLEDAVE
GIVSIEGLKRRLSDFHWPDTLPRLPDARTDIENFKIGVRAYQQNTMKPFG
TAVGKLLRSPGNPRGVPDLVIERAGQDTLGVSTSLVKPFGGRVIYAEEMA
GRRYTFYAPQVWTRQRRIYMPSAEIFGTHLCNAYEVTMMNEMVAAGLLDV
TEPTMVPWEGLPEAHQAMWDNRHSGATYVVNHALPAMGLTTKDELLEYWV
AAQ
3D structure
PDB6eqo The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite.
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A957 G1004 E1007 E1027 G1035
Catalytic site (residue number reindexed from 1) A917 G964 E967 E987 G995
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase.
6.2.1.1: acetate--CoA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0003987 acetate-CoA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006085 acetyl-CoA biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6eqo, PDBe:6eqo, PDBj:6eqo
PDBsum6eqo
PubMed30374166
UniProtA3WE14

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