Structure of PDB 2w0u Chain D

Receptor sequence
>2w0uD (length=334) Species: 9606 (Homo sapiens) [Search protein sequence]
RLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRM
LRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGT
GMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYK
AIFVTVDTPYLGNRLDDVRNRFKLGLAAYVAKAIDPSISWEDIKWLRRLT
SLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIV
EAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGV
QDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKN
3D structure
PDB2w0u Structure of Human Glycolate Oxidase in Complex with the Inhibitor 4-Carboxy-5-[(4-Chlorophenyl)Sulfanyl]-1,2,3-Thiadiazole.
ChainD
Resolution2.84 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S108 Y132 T158 D160 K236 H260
Catalytic site (residue number reindexed from 1) S105 Y129 T155 D157 K207 H231
Enzyme Commision number 1.1.3.15: (S)-2-hydroxy-acid oxidase.
1.2.3.5: glyoxylate oxidase.
Interaction with ligand
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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Cellular Component
External links
PDB RCSB:2w0u, PDBe:2w0u, PDBj:2w0u
PDBsum2w0u
PubMed20054120
UniProtQ9UJM8|HAOX1_HUMAN 2-Hydroxyacid oxidase 1 (Gene Name=HAO1)

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