Structure of PDB 1dtw Chain A

Receptor sequence
>1dtwA (length=382) Species: 9606 (Homo sapiens) [Search protein sequence]
PQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEK
VLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNT
DLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERH
FVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFN
FAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGN
DVFAVYNATKEARRRAVAENQPFLIEAMTYRIGHHSTSDDSSAYRHPISR
LRHYLLSQGWWDEEQEKAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVY
QEMPAQLRKQQESLARHLQTYGEHYPLDHFDK
3D structure
PDB1dtw Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.
ChainA
Resolution2.7 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) E70 S156 R281 H285 S286 Y294
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 MG A E193 N222 Y224 E187 N216 Y218
BS02 K A S161 S162 P163 T166 Q167 S155 S156 P157 T160 Q161
BS03 TPP A Q112 Y113 R114 L164 G192 E193 G194 A195 R220 N222 Y224 A225 I226 H291 Q106 Y107 R108 L158 G186 E187 G188 A189 R214 N216 Y218 A219 I220 H285
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:1dtw, PDBe:1dtw, PDBj:1dtw
PDBsum1dtw
PubMed10745006
UniProtP12694|ODBA_HUMAN 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (Gene Name=BCKDHA)

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