Structure of PDB 2r0n Chain A

Receptor sequence
>2r0nA (length=390) Species: 9606 (Homo sapiens) [Search protein sequence]
EFDWQDPLVLEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREI
ISEMGELGVLGPTIKGYGCAGVSSVAYGLLARELERVDSGYRSAMSVQSS
LVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAH
YNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEKGMRGLS
APRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNARYG
IAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLG
LHACLQLGRLKDQDKAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISD
EYHVIRHAMNLEAVNTYEGTHDIHALILGRAITGIQAFTA
3D structure
PDB2r0n The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L135 T136 A249 E370 R382
Catalytic site (residue number reindexed from 1) L133 T134 A247 E368 R380
Enzyme Commision number 1.3.8.6: glutaryl-CoA dehydrogenase (ETF).
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 A F133 L135 T136 G141 S142 W168 I169 T170 Y369 T372 D374 F131 L133 T134 G139 S140 W166 I167 T168 Y367 T370 D372
BS02 TGC A R94 S95 V99 P144 G240 F243 L246 N247 P320 Y369 E370 I379 R92 S93 V97 P142 G238 F241 L244 N245 P318 Y367 E368 I377
Gene Ontology
Molecular Function
GO:0000062 fatty-acyl-CoA binding
GO:0003995 acyl-CoA dehydrogenase activity
GO:0004361 glutaryl-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:0006568 tryptophan metabolic process
GO:0006637 acyl-CoA metabolic process
GO:0019395 fatty acid oxidation
GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase
GO:0046949 fatty-acyl-CoA biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2r0n, PDBe:2r0n, PDBj:2r0n
PDBsum2r0n
PubMed18020372
UniProtQ92947|GCDH_HUMAN Glutaryl-CoA dehydrogenase, mitochondrial (Gene Name=GCDH)

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