Structure of PDB 2xq1 Chain N

Receptor sequence
>2xq1N (length=491) [Search protein sequence]
ANPPVFTTSQGCPVSDPFTTQRIPLDSTGYKYAPPIGPLLLQDFKLIDTL
SHFDRERIPERVVHAKGAGAYGVFEVTDDITDVCSAKFLDTVGKKTRIFT
RFSTVGGEKGSADTARDPRGFATKFYTEDGNLDLVYNNTPIFFIRDPIKF
PHFIHTQKRNPATNLKDPNMFWDYLTANDESLHQVMYLFSNRGTPASYRT
MNGYSGHTYKWYNSKGEWVYVQVHFIANQGVHNLLDEEAGRLAGEDPDHS
TRDLWEAIEKGDYPSWECYIQTMTLEQSKKLPFSVFDLTKVWPHKDFPLR
HFGRFTLNENPKNYYAETEQIAFSPSHTVPGMEPSNDPVLQSRLFSYPDT
HRHRLGPNYHQIPVNCPLKSGSFNPINRDGPMCVDGNLGGTPNYANAYNC
PIQYAVSDEKYTGEVVPYHWEHTDYDYFQPKMFWKVLGRTPGEQESLVKN
VANHVSAADEFIQDRVYEYFSKAEPIIGDLIRKKVQELKRK
3D structure
PDB2xq1 Structural Features of Peroxisomal Catalase from the Yeast Hansenula Polymorpha
ChainN
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.6: catalase.
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 HEM N R62 V63 V64 H65 R102 V136 N138 F151 F324 V340 R344 Y348 T351 H352 R355 R61 V62 V63 H64 R101 V135 N137 F150 F323 V339 R343 Y347 T350 H351 R354
Gene Ontology
Molecular Function
GO:0004096 catalase activity
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006979 response to oxidative stress
GO:0042542 response to hydrogen peroxide
GO:0042744 hydrogen peroxide catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xq1, PDBe:2xq1, PDBj:2xq1
PDBsum2xq1
PubMed21795810
UniProtP30263|CATA_PICAN Peroxisomal catalase (Gene Name=PXP9)

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