Structure of PDB 5qid Chain A

Receptor sequence
>5qidA (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
RLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRM
LRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGT
GMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYK
AIFVTVDTPYLGNRLDDVRNRFKLPPQLRMKNFDSGLAAYVAKAIDPSIS
WEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGV
PATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIV
WGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRK
3D structure
PDB5qid PanDDA analysis group deposition of models with modelled events (e.g. bound ligands)
ChainA
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y132 D160 H260
Catalytic site (residue number reindexed from 1) Y129 D157 H242
Enzyme Commision number 1.1.3.15: (S)-2-hydroxy-acid oxidase.
1.2.3.5: glyoxylate 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 Y26 Y27 A79 T80 A81 S108 Q130 Y132 K236 H260 G261 R263 D291 G292 R295 G314 R315 Y23 Y24 A76 T77 A78 S105 Q127 Y129 K218 H242 G243 R245 D273 G274 R277 G296 R297
BS02 GWY A T60 E338 R341 T57 E320 R323
Gene Ontology
Molecular Function
GO:0003973 (S)-2-hydroxy-acid oxidase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0047969 glyoxylate oxidase activity
Biological Process
GO:0001561 fatty acid alpha-oxidation
GO:0006545 glycine biosynthetic process
GO:0006979 response to oxidative stress
GO:0008652 amino acid biosynthetic process
GO:0046296 glycolate catabolic process
Cellular Component
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Cellular Component
External links
PDB RCSB:5qid, PDBe:5qid, PDBj:5qid
PDBsum5qid
PubMed
UniProtQ9UJM8|HAOX1_HUMAN 2-Hydroxyacid oxidase 1 (Gene Name=HAO1)

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