Structure of PDB 3eya Chain D

Receptor sequence

>3eyaD (length=520) Species: 562 (Escherichia coli) [Search protein sequence]

KQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEE
VAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAH
IPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLN
RGVSVVVLPGDVALKPAPEGATMHWYHAPQPVVTPEEEELRKLAQLLRYS
SNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGMT
GLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGAH
SKVDMALVGDIKSTLRALLPLVEEKADRKFLDKALEDYRDARKGLDDLAK
PSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLG
SFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMKL
PVKIVVFNNSVLGFVGTELHDTNFARIAEACGITGIRVEKASEVDEALQR
AFSIDGPVLVDVVVAKEELA

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)	V23 G25 D26 S27 L28 E49 S72 F111 Q112 G160 L252 A279 V379 G405 M407 D432 N459 V461 L462 F464 V465 K516
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	D	T25 E50 S73 H80	T24 E49 S72 H79
BS02	TPP	D	G381 T382 M408 G432 D433 G434 G435 N460 V462 L463 G464 F465 V466	G380 T381 M407 G431 D432 G433 G434 N459 V461 L462 G463 F464 V465
BS03	FAD	D	H92 G209 S210 G211 A233 L234 R235 T251 G252 I254 G273 T274 Q275 F276 Y278 D292 I293 S297 D311 I312 F403 N404	H91 G208 S209 G210 A232 L233 R234 T250 G251 I253 G272 T273 Q274 F275 Y277 D291 I292 S296 D310 I311 F402 N403
BS04	MG	D	D433 N460 V462	D432 N459 V461

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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