Structure of PDB 3mpj Chain B Binding Site BS01
Receptor Information
>3mpj Chain B (length=393) Species:
897
(Desulfococcus multivorans) [
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MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELG
FFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYT
ILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDH
WLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTS
NLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAA
AGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARL
LAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTE
YPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANRKGHH
Ligand information
>3mpj Chain Y (length=8) Species:
897
(Desulfococcus multivorans) [
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KGHHHHHH
Receptor-Ligand Complex Structure
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PDB
3mpj
Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme a dehydrogenases.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
H36 F37 Y39 A164 Q165 D167 N193
Binding residue
(residue number reindexed from 1)
H36 F37 Y39 A164 Q165 D167 N193
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).
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:3mpj
,
PDBe:3mpj
,
PDBj:3mpj
PDBsum
3mpj
PubMed
20486657
UniProt
C3UVB0
|ACD_DESML Glutaryl-CoA dehydrogenase (Gene Name=Acd)
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