Structure of PDB 1zmc Chain F

Receptor sequence

>1zmcF (length=471) Species: 9606 (Homo sapiens) [Search protein sequence]

PIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPS
KALLNNSHYYHMAHGTDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGI
AHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVT
PFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGAD
VTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGK
IDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIP
VNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNC
VPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGM
VKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHP
TLSEAFREANLAASFGKSINF

3D structure

PDB

1zmc Crystal Structure of Human Dihydrolipoamide Dehydrogenase: NAD(+)/NADH Binding and the Structural Basis of Disease-causing Mutations

Chain

Resolution

2.53 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)	L38 C42 C47 S50 V185 E189 H447 H449 E454
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	F	I12 G13 G15 P16 G17 E36 K37 N38 G43 T44 C45 G49 C50 K54 Y118 G119 T148 G149 I189 F283 D320 M326 L327 A328 H329	I9 G10 G12 P13 G14 E33 K34 N35 G40 T41 C42 G46 C47 K51 Y115 G116 T145 G146 I186 F280 D317 M323 L324 A325 H326
BS02	NAD	F	I184 G185 E208 F209 L210 G215 V216 V243 I278 G279	I181 G182 E205 F206 L207 G212 V213 V240 I275 G276

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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1zmc, PDBe:1zmc, PDBj:1zmc
PDBsum	1zmc
PubMed	15946682
UniProt	P09622\|DLDH_HUMAN Dihydrolipoyl dehydrogenase, mitochondrial (Gene Name=DLD)

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