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BioLiP

Structure of PDB 1y9d Chain D

Receptor sequence
>1y9dD (length=560) Species: 1590 (Lactiplantibacillus plantarum) [Search protein sequence]
TNILAGAAVIKVLEAWGVDHLYGIPGGSINSIMDALSAERDRIHYIQVRH
EEVGAMAAAADAKLTGKIGVCFGSAGPGGTHLMNGLYDAREDHVPVLALI
GQFGTTGEMNENPIYADVADYNVTAVNAATLPHVIDEAIRRAYAHQGVAV
VQIPVDLPWQQIPAEDWYASAPEPDVQAVTRLTQTLLAAERPLIYYGIGA
RKAGKELEQLSKTLKIPLMSTYPAKGIVADRYPAYLGSANRAAQKPANEA
LAQADVVLFVGNNYNTRYFLQIDIDPAKLGKRHKTDIAVLADAQKTLAAI
LAQVSERESTPWWQANLANVKNWRAYLASLEDKQEGPLQAYQVLRAVNKI
AEPDAIYSIDVGDINLNANRHLKLTPSNRHITSNLFATMGVGIPGAIAAK
LNYPERQVFNLAGDGGASMTMQDLATQVQYHLPVINVVFTNCQYGFIKDE
QEDTNQNDFIGVEFNDIDFSKIADGVHMQAFRVNKIEQLPDVFEQAKAIA
QHEPVLIDAVITGDRPLPAEKLRLDSAMSSAADIEAFKQRYEAQDLQPLS
TYLKQFGLDD
3D structure
PDB1y9d The role of Val-265 for Flavin Adenine Dinulceotide (FAD) binding in pyruvate oxidase: FTIR, kinetic and crystallographic studies on the enzyme variant V265A
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I32 G34 G35 S36 I37 E59 S82 E123 V170 R264 V394 A420 M422 D447 N474 Q476 Y477 F479 I480 E483 G546
Catalytic site (residue number reindexed from 1) I24 G26 G27 S28 I29 E51 S74 E108 V155 R241 V361 A387 M389 D414 N441 Q443 Y444 F446 I447 E450 G513
Enzyme Commision number 1.2.3.3: pyruvate oxidase.
Interaction with ligand
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:1y9d, PDBe:1y9d, PDBj:1y9d
PDBsum1y9d
PubMed15794646
UniProtP37063|POXB_LACPL Pyruvate oxidase (Gene Name=pox5)

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