Structure of PDB 1zy8 Chain B

Receptor sequence
>1zy8B (length=474) Species: 9606 (Homo sapiens) [Search protein sequence]
ADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGC
IPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALT
GGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGS
EVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRL
GADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKS
DGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRG
RIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHID
YNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADT
DGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCH
AHPTLSEAFREANLAASFGKSINF
3D structure
PDB1zy8 How Dihydrolipoamide Dehydrogenase-binding Protein Binds Dihydrolipoamide Dehydrogenase in the Human Pyruvate Dehydrogenase Complex.
ChainB
Resolution2.59 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) L41 C45 C50 S53 V188 E192 H450 H452 E457
Enzyme Commision number 1.8.1.4: dihydrolipoyl dehydrogenase.
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 B I12 G15 P16 E36 K37 N38 G43 T44 C45 G49 C50 K54 T148 G149 I189 F283 G319 D320 M326 L327 A328 Y359 I12 G15 P16 E36 K37 N38 G43 T44 C45 G49 C50 K54 T148 G149 I189 F283 G319 D320 M326 L327 A328 Y359
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:1zy8, PDBe:1zy8, PDBj:1zy8
PDBsum1zy8
PubMed16263718
UniProtP09622|DLDH_HUMAN Dihydrolipoyl dehydrogenase, mitochondrial (Gene Name=DLD)

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