Structure of PDB 2ezu Chain A Binding Site BS01

Receptor Information

>2ezu Chain A (length=585) Species: 1590 (Lactiplantibacillus plantarum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TNILAGAAVIKVLEAWGVDHLYGIPGGSINSIMDALSAERDRIHYIQVRH
EEVGAMAAAADAKLTGKIGVCFGSAGPGGTHLMNGLYDAREDHVPVLALI
GQFGTTGMNMDTFQEMNENPIYADVADYNVTAVNAATLPHVIDEAIRRAY
AHQGVAVVQIPVDLPWQQIPAEDWYASANSYQTPLLPEPDVQAVTRLTQT
LLAAERPLIYYGIGARKAGKELEQLSKTLKIPLMSTYPAKGIVADRYPAY
LGSANRVAQKPANEALAQADVVLFVGNNYPFAEVSKAFKNTRYFLQIDID
PAKLGKRHKTDIAVLADAQKTLAAILAQVSERESTPWWQANLANVKNWRA
YLASLEDKQEGPLQAYQVLRAVNKIAEPDAIYSIDVGDINLNANRHLKLT
PSNRHITSNLFATMGVGIPGAIAAKLNYPERQVFNLAGDGGASMTMQDLA
TQVQYHLPVINVVFTNCQYGWIKDEQEDTNQNDFIGVEFNDIDFSKIADG
VHMQAFRVNKIEQLPDVFEQAKAIAQHEPVLIDAVITGDRPLPAEKLRLD
SAMSSAADIEAFKQRYEAQDLQPLSTYLKQFGLDD

Ligand information

Ligand ID

InChI

InChI=1S/Mg/q+2

InChIKey

JLVVSXFLKOJNIY-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mg+2]
CACTVS 3.341	[Mg++]

Formula

Name

MAGNESIUM ION

PDB chain

2ezu Chain A Residue 1610 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2ezu The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography.
Resolution	2.16 Å
Binding residue (original residue number in PDB)	D447 N474 Q476
Binding residue (residue number reindexed from 1)	D439 N466 Q468
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	I32 G34 G35 S36 I37 E59 S82 F121 Q122 E123 V170 R264 E291 V394 A420 M422 D447 N474 Q476 Y477 W479 I480 E483 G546
Catalytic site (residue number reindexed from 1)	I24 G26 G27 S28 I29 E51 S74 F113 Q114 E115 V162 R256 E283 V386 A412 M414 D439 N466 Q468 Y469 W471 I472 E475 G538
Enzyme Commision number	1.2.3.3: pyruvate oxidase.

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0016491	oxidoreductase activity
GO:0030976	thiamine pyrophosphate binding
GO:0046872	metal ion binding
GO:0047112	pyruvate oxidase activity

View graph for
Molecular Function

External links

PDB	RCSB:2ezu, PDBe:2ezu, PDBj:2ezu
PDBsum	2ezu
PubMed	16680160
UniProt	P37063\|POXB_LACPL Pyruvate oxidase (Gene Name=pox5)

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