Structure of PDB 1gyl Chain A

Receptor sequence
>1gylA (length=352) Species: 3562 (Spinacia oleracea) [Search protein sequence]
MEITNVNEYEAIAKQKLPKMVYDFYASGAEDQWTLAENRNAFSRILFRPR
ILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAG
TIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFK
AIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKGLSSYVAGQI
DRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGAR
QLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFI
GRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAAD
WD
3D structure
PDB1gyl Involvement of Tyr24 and Trp108 in substrate binding and substrate specificity of glycolate oxidase.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S106 Y129 T155 D157 K230 H254
Catalytic site (residue number reindexed from 1) S106 Y129 T155 D157 K223 H247
Enzyme Commision number 1.1.3.15: (S)-2-hydroxy-acid oxidase.
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 FMN A F24 A76 P77 A79 S106 Q127 Y129 T155 K230 H254 R257 D285 G286 R289 G308 R309 F24 A76 P77 A79 S106 Q127 Y129 T155 K223 H247 R250 D278 G279 R282 G301 R302
Gene Ontology
Molecular Function
GO:0003973 (S)-2-hydroxy-acid oxidase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0009853 photorespiration
GO:0009854 oxidative photosynthetic carbon pathway
GO:0051707 response to other organism
Cellular Component
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1gyl, PDBe:1gyl, PDBj:1gyl
PDBsum1gyl
PubMed7705356
UniProtP05414|GOX_SPIOL Glycolate oxidase

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