Structure of PDB 1al8 Chain A

Receptor sequence
>1al8A (length=344) Species: 3562 (Spinacia oleracea) [Search protein sequence]
MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPR
ILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAG
TIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFK
AIALTVDTPRLIKNRFVLPPFLTLKNFEGIDLGLSSYVAGQIDRSLSWKD
VAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPAT
IMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSL
AAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWD
3D structure
PDB1al8 Three-dimensional structures of glycolate oxidase with bound active-site inhibitors.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 K215 H239
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 Y25 P77 T78 A79 S106 Q127 Y129 T155 K230 H254 R257 D285 G286 R289 G308 R309 Y25 P77 T78 A79 S106 Q127 Y129 T155 K215 H239 R242 D270 G271 R274 G293 R294
BS02 DHP A Y24 W108 Y129 F172 H254 R257 Y24 W108 Y129 F166 H239 R242 MOAD: Ki=4.8uM
PDBbind-CN: -logKd/Ki=5.32,Ki=4.8uM
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1al8, PDBe:1al8, PDBj:1al8
PDBsum1al8
PubMed9144771
UniProtP05414|GOX_SPIOL Glycolate oxidase

[Back to BioLiP]