Structure of PDB 1ivh Chain D

Receptor sequence
>1ivhD (length=387) Species: 9606 (Homo sapiens) [Search protein sequence]
VDDAINGLSEEQRQLRQTMAKFLQEHLAPKAQEIDRSNEFKNLREFWKQL
GNLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCI
NQLVRNGNEAQKEKYLPKLISGEYIGALAMSEPNAGSDVVSMKLKAEKKG
NHYILNGNKFWITNGPDADVLIVYAKTDLAAVPASRGITAFIVEKGMPGF
STSKKLDKLGMRGSNTCELIFEDCKIPAANILGHENKGVYVLMSGLDLER
LVLAGGPLGLMQAVLDHTIPYLHVREAFGQKIGHFQLMQGKMADMYTRLM
ACRQYVYNVAKACDEGHCTAKDCAGVILYSAECATQVALDGIQCFGGNGY
INDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNAD
3D structure
PDB1ivh Structure of human isovaleryl-CoA dehydrogenase at 2.6 A resolution: structural basis for substrate specificity,.
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M135 S136 E254 A375 R387
Catalytic site (residue number reindexed from 1) M130 S131 E249 A370 R382
Enzyme Commision number 1.3.8.1: short-chain acyl-CoA dehydrogenase.
1.3.8.4: isovaleryl-CoA dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003995 acyl-CoA dehydrogenase activity
GO:0005515 protein binding
GO:0008470 3-methylbutanoyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0016937 short-chain fatty acyl-CoA dehydrogenase activity
GO:0042802 identical protein binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006552 L-leucine catabolic process
GO:0006631 fatty acid metabolic process
GO:0009083 branched-chain amino acid catabolic process
GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase
Cellular Component
GO:0005654 nucleoplasm
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:1ivh, PDBe:1ivh, PDBj:1ivh
PDBsum1ivh
PubMed9214289
UniProtP26440|IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial (Gene Name=IVD)

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