Structure of PDB 3mpj Chain D

Receptor sequence
>3mpjD (length=390) Species: 897 (Desulfococcus multivorans) [Search protein sequence]
MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELG
FFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYT
ILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDH
WLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTS
NLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAA
AGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARL
LAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTE
YPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANRK
3D structure
PDB3mpj Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme a dehydrogenases.
ChainD
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I128 T129 T245 E367 L379
Catalytic site (residue number reindexed from 1) I128 T129 T245 E367 L379
Enzyme Commision number 1.3.99.32: glutaryl-CoA dehydrogenase (acceptor).
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 FAD D F126 I128 T129 G134 S135 W159 I160 S161 V366 S369 N371 M375 F126 I128 T129 G134 S135 W159 I160 S161 V366 S369 N371 M375
BS02 FAD D R271 F274 I278 F281 N284 R340 I341 A344 R271 F274 I278 F281 N284 R340 I341 A344
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003995 acyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0009056 catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3mpj, PDBe:3mpj, PDBj:3mpj
PDBsum3mpj
PubMed20486657
UniProtC3UVB0|ACD_DESML Glutaryl-CoA dehydrogenase (Gene Name=Acd)

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