Structure of PDB 1v59 Chain A

Receptor sequence

>1v59A (length=478) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

TINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCI
PSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLTG
GIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNII
VATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGS
VYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISA
KRNDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLE
VDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEMLKTG
HGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAK
TNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDV
ARVCHAHPTLSEAFKEANMAAYDKAIHC

3D structure

PDB

1v59 Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+

Chain

Resolution

2.2 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	L40 C44 C49 S52 I193 E197 T349 H455 H457 E462
Catalytic site (residue number reindexed from 1)	L40 C44 C49 S52 I193 E197 T349 H455 H457 E462
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	A	G14 P15 A16 E35 K36 R37 G42 T43 C44 G48 C49 K53 N117 G118 T153 G154 R285 Y288 G324 D325 M331 L332 A333 H334 Y364	G14 P15 A16 E35 K36 R37 G42 T43 C44 G48 C49 K53 N117 G118 T153 G154 R285 Y288 G324 D325 M331 L332 A333 H334 Y364
BS02	NAD	A	I189 G190 E213 F214 K246 V283	I189 G190 E213 F214 K246 V283

Gene Ontology

	Molecular Function
GO:0004148	dihydrolipoyl dehydrogenase activity
GO:0004375	glycine dehydrogenase (decarboxylating) activity
GO:0004591	oxoglutarate dehydrogenase (succinyl-transferring) activity
GO:0004738	pyruvate 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:0050660	flavin adenine dinucleotide binding

	Biological Process
GO:0006086	acetyl-CoA biosynthetic process from pyruvate
GO:0006090	pyruvate metabolic process
GO:0006099	tricarboxylic acid cycle
GO:0006103	2-oxoglutarate metabolic process
GO:0006546	glycine catabolic process
GO:0006550	isoleucine catabolic process
GO:0006552	L-leucine catabolic process
GO:0006564	L-serine biosynthetic process
GO:0006574	valine catabolic process
GO:0042743	hydrogen peroxide metabolic process

	Cellular Component
GO:0005739	mitochondrion
GO:0005759	mitochondrial matrix
GO:0005960	glycine cleavage complex
GO:0042645	mitochondrial nucleoid
GO:0045252	oxoglutarate dehydrogenase complex
GO:0045254	pyruvate dehydrogenase complex

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1v59, PDBe:1v59, PDBj:1v59
PDBsum	1v59
PubMed
UniProt	P09624\|DLDH_YEAST Dihydrolipoyl dehydrogenase, mitochondrial (Gene Name=LPD1)

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