Structure of PDB 1olx Chain A

Receptor sequence
>1olxA (length=391) Species: 9606 (Homo sapiens) [Search protein sequence]
DKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPK
EKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALD
NTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKE
RHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAG
FNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVD
GNDVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRNYW
DKQDHPISRLRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPN
PNLLFSDVYQEMPAQLRKQQESLARHLQTYGEHYPLDHFDK
3D structure
PDB1olx Roles of His291-Alpha and His146-Beta' in the Reductive Acylation Reaction Catalyzed by Human Branched-Chain Alpha-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E76 S162 R287 H291 S292 Y300
Catalytic site (residue number reindexed from 1) E72 S158 R283 H287 S288 Y296
Enzyme Commision number 1.2.4.4: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
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 MN A E193 N222 Y224 E189 N218 Y220
BS02 TPP A Q112 Y113 R114 L164 G192 E193 G194 A195 R220 N222 Y224 A225 I226 H291 Q108 Y109 R110 L160 G188 E189 G190 A191 R216 N218 Y220 A221 I222 H287
Gene Ontology
Molecular Function
GO:0003863 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
GO:0047101 branched-chain alpha-keto acid dehydrogenase activity
Biological Process
GO:0009083 branched-chain amino acid catabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0045252 oxoglutarate dehydrogenase complex
GO:0160157 branched-chain alpha-ketoacid dehydrogenase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1olx, PDBe:1olx, PDBj:1olx
PDBsum1olx
PubMed12902323
UniProtP12694|ODBA_HUMAN 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (Gene Name=BCKDHA)

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