Structure of PDB 3eya Chain L

Receptor sequence

>3eyaL (length=523) Species: 562 (Escherichia coli) [Search protein sequence]

MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHE
EVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAA
HIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVL
NRGVSVVVLPGDVALKPAPEGATMHWYHAPQPVVTPEEEELRKLAQLLRY
SSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGM
TGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGA
HSKVDMALVGDIKSTLRALLPLVEEKADRKFLDKALEDYRDARKGLDDLA
KPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLL
GSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMK
LPVKIVVFNNSVLGFVGTELHDTNFARIAEACGITGIRVEKASEVDEALQ
RAFSIDGPVLVDVVVAKEELAIP

3D structure

PDB

3eya Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli.

Chain

Resolution

2.5 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	V24 G26 D27 S28 L29 E50 S73 F112 Q113 G161 L253 A280 V380 G406 M408 D433 N460 V462 L463 F465 V466 K529
Catalytic site (residue number reindexed from 1)	V24 G26 D27 S28 L29 E50 S73 F112 Q113 G161 L253 A280 V380 G406 M408 D433 N460 V462 L463 F465 V466 K517
Enzyme Commision number	1.2.5.1: pyruvate dehydrogenase (quinone).

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)
BS01	TPP	L	T25 E50 S73 P76 G77 H80	T25 E50 S73 P76 G77 H80
BS02	TPP	L	G381 T382 M408 G432 D433 G434 G435 N460 V462 L463 G464 F465	G381 T382 M408 G432 D433 G434 G435 N460 V462 L463 G464 F465
BS03	FAD	L	H92 G209 S210 G211 A233 L234 R235 T251 G252 I254 G273 T274 Q275 F276 Y278 D292 I293 S297 D311 I312 F403 N404	H92 G209 S210 G211 A233 L234 R235 T251 G252 I254 G273 T274 Q275 F276 Y278 D292 I293 S297 D311 I312 F403 N404
BS04	MG	L	D433 N460 V462	D433 N460 V462

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0008289	lipid binding
GO:0016491	oxidoreductase activity
GO:0030976	thiamine pyrophosphate binding
GO:0042802	identical protein binding
GO:0046872	metal ion binding
GO:0048039	ubiquinone binding
GO:0050660	flavin adenine dinucleotide binding
GO:0052737	pyruvate dehydrogenase (quinone) activity

	Biological Process
GO:0006090	pyruvate metabolic process
GO:0019752	carboxylic acid metabolic process
GO:0042867	pyruvate catabolic process

	Cellular Component
GO:0005829	cytosol
GO:0005886	plasma membrane
GO:0032991	protein-containing complex

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Molecular Function

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Cellular Component

External links

PDB	RCSB:3eya, PDBe:3eya, PDBj:3eya
PDBsum	3eya
PubMed	18988747
UniProt	P07003\|POXB_ECOLI Pyruvate dehydrogenase [ubiquinone] (Gene Name=poxB)

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