Structure of PDB 3mpj Chain G

Receptor sequence

>3mpjG (length=389) Species: 897 (Desulfococcus multivorans)

MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELG
FFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYT
ILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDH
WLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTS
NLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAA
AGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARL
LAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTE
YPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANR

3D structure

• PDB: 3mpj Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme a dehydrogenases.
• Chain: G
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L379
• Catalytic site (residue number reindexed from 1): 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	G	R271 F274 I278 F281 R340 I341 G343 A344	R271 F274 I278 F281 R340 I341 G343 A344
BS02	FAD	G	F126 I128 T129 G134 S135 W159 I160 S161 M365 V366 S369 N371 M375	F126 I128 T129 G134 S135 W159 I160 S161 M365 V366 S369 N371 M375

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

External links

• PDB: RCSB:3mpj, PDBe:3mpj, PDBj:3mpj
• PDBsum: 3mpj
• PubMed: 20486657
• UniProt: C3UVB0|ACD_DESML Glutaryl-CoA dehydrogenase (Gene Name=Acd)