Structure of PDB 6i4p Chain B

Receptor sequence
>6i4pB (length=481) Species: 9606 (Homo sapiens) [Search protein sequence]
VLFQGPGADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGG
TCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKS
TAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKN
ILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVEL
CSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKV
TGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELG
IELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMA
GGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSR
AKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCE
DIARVCHAHPTLSEAFREANLAASFGKSINF
3D structure
PDB6i4p Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants.
ChainB
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C45 C50 S53 V188 E192 H452 E457
Catalytic site (residue number reindexed from 1) C52 C57 S60 V195 E199 H459 E464
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 G17 E36 K37 N38 G43 T44 C45 G49 C50 K54 Y118 G119 T148 G149 I189 R280 F283 G319 D320 M326 L327 A328 H329 I19 G22 P23 G24 E43 K44 N45 G50 T51 C52 G56 C57 K61 Y125 G126 T155 G156 I196 R287 F290 G326 D327 M333 L334 A335 H336
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:6i4p, PDBe:6i4p, PDBj:6i4p
PDBsum6i4p
PubMed31334547
UniProtP09622|DLDH_HUMAN Dihydrolipoyl dehydrogenase, mitochondrial (Gene Name=DLD)

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