Structure of PDB 3zwb Chain B

Receptor sequence
>3zwbB (length=721) Species: 10116 (Rattus norvegicus) [Search protein sequence]
GSHMAEYLRLPHSLAMIRLCNPPVNAVSPTVIREVRNGLQKAGSDHTVKA
IVICGANGNFCAGADIHGFSAFTPGLALGSLVDEIQRYQKPVLAAIQGVA
LGGGLELALGCHYRIANAKARVGLPAVTLGILPGARGTQLLPRVVGVPVA
LDLITSGKYLSADEALRLGILDAVVKSDPVEEAIKFAQKIIDKPIEPRRI
FNKPVPSLPNMDSVFAEAIAKVRKQYPGVLAPETCVRSIQASVKHPYEVG
IKEEEKLFMYLRASGQAKALQYAFFAEKSANKWSTPSGASWKTASAQPVS
SVGVLGLGTMGRGIAISFARVGISVVAVESDPKQLDAAKKIITFTLEKEA
SRAHQNGQASAKPKLRFSSSTKELSTVDLVVEAVFEDMNLKKKVFAELSA
LCKPGAFLCTNTSALNVDDIASSTDRPQLVIGTHFFSPAHVMRLLEVIPS
RYSSPTTIATVMSLSKKIGKIGVVVGNCYGFVGNRMLAPYYNQGFFLLEE
GSKPEDVDGVLEEFGFKMGPFRVSDLAGLDVGWKIRKGQGLTGPSLPPGT
PVRKRGNSRYSPLGDMLCEAGRFGQKTGKGWYQYDKPLGRIHKPDPWLST
FLSQYREVHHIEQRTISKEEILERCLYSLINEAFRILEEGMAARPEHIDV
IYLHGYGWPRHKGGPMFYAASVGLPTVLEKLQKYYRQNPDIPQLEPSDYL
RRLVAQGSPPLKEWQSLAGPH
3D structure
PDB3zwb The Isomerase and Hydratase Reaction Mechanism of the Crotonase Active Site of the Multifunctional Enzyme (Type-1), as Deduced from Structures of Complexes with 3S-Hydroxy- Acyl-Coa.
ChainB
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A61 G76 G100 E103 P122 A123 P130 G131 S410 H431 E443 N481
Catalytic site (residue number reindexed from 1) A64 G79 G103 E106 P125 A126 P133 G134 S413 H434 E446 N484
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase.
4.2.1.17: enoyl-CoA hydratase.
5.3.3.8: Delta(3)-Delta(2)-enoyl-CoA isomerase.
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 TC6 B P20 V21 A59 G60 A61 D62 I63 F66 G100 E103 P130 G131 A132 Y156 F255 K275 K463 P23 V24 A62 G63 A64 D65 I66 F69 G103 E106 P133 G134 A135 Y159 F258 K278 K466
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0004165 delta(3)-delta(2)-enoyl-CoA isomerase activity
GO:0004300 enoyl-CoA hydratase activity
GO:0016491 oxidoreductase activity
GO:0016509 long-chain-3-hydroxyacyl-CoA dehydrogenase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0016863 intramolecular oxidoreductase activity, transposing C=C bonds
GO:0019899 enzyme binding
GO:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
Cellular Component
GO:0005777 peroxisome
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:3zwb, PDBe:3zwb, PDBj:3zwb
PDBsum3zwb
PubMed23351063
UniProtP07896|ECHP_RAT Peroxisomal bifunctional enzyme (Gene Name=Ehhadh)

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