Structure of PDB 1zmd Chain E

Receptor sequence
>1zmdE (length=473) Species: 9606 (Homo sapiens) [Search protein sequence]
DQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCI
PSKALLNNSHYYHMAHGTDFASRGIEMSEVRLNLDKMMEQKSTAVKALTG
GIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSE
VTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLG
ADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSD
GKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGR
IPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDY
NCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTD
GMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHA
HPTLSEAFREANLAASFGKSINF
3D structure
PDB1zmd Crystal Structure of Human Dihydrolipoamide Dehydrogenase: NAD+/NADH Binding and the Structural Basis of Disease-causing Mutations
ChainE
Resolution2.08 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L41 C45 C50 S53 V188 E192 H450 H452 E457
Catalytic site (residue number reindexed from 1) L40 C44 C49 S52 V187 E191 H449 H451 E456
Enzyme Commision number 1.8.1.4: dihydrolipoyl dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004148 dihydrolipoyl dehydrogenase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0034604 pyruvate dehydrogenase (NAD+) activity
GO:0047101 branched-chain alpha-keto acid dehydrogenase activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0006086 acetyl-CoA biosynthetic process from pyruvate
GO:0006120 mitochondrial electron transport, NADH to ubiquinone
GO:0006508 proteolysis
GO:0007369 gastrulation
GO:0009083 branched-chain amino acid catabolic process
GO:0042391 regulation of membrane potential
GO:0048240 sperm capacitation
Cellular Component
GO:0001669 acrosomal vesicle
GO:0005634 nucleus
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005929 cilium
GO:0031410 cytoplasmic vesicle
GO:0031514 motile cilium
GO:0043159 acrosomal matrix
GO:0045252 oxoglutarate dehydrogenase complex
GO:0045254 pyruvate dehydrogenase complex
GO:0160157 branched-chain alpha-ketoacid dehydrogenase complex
GO:0160167 oxoadipate dehydrogenase complex
GO:1902493 acetyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1zmd, PDBe:1zmd, PDBj:1zmd
PDBsum1zmd
PubMed15946682
UniProtP09622|DLDH_HUMAN Dihydrolipoyl dehydrogenase, mitochondrial (Gene Name=DLD)

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