Structure of PDB 2xq1 Chain G

Receptor sequence
>2xq1G (length=491) [Search protein sequence]
PPVFTTSQGCPVSDPFTTQRIPLDSTGYKYAPPIGPLLLQDFKLIDTLSH
FDRERIPERVVHAKGAGAYGVFEVTDDITDVCSAKFLDTVGKKTRIFTRF
STVGGEKGSADTARDPRGFATKFYTEDGNLDLVYNNTPIFFIRDPIKFPH
FIHTQKRNPATNLKDPNMFWDYLTANDESLHQVMYLFSNRGTPASYRTMN
GYSGHTYKWYNSKGEWVYVQVHFIANQGVHNLLDEEAGRLAGEDPDHSTR
DLWEAIEKGDYPSWECYIQTMTLEQSKKLPFSVFDLTKVWPHKDFPLRHF
GRFTLNENPKNYYAETEQIAFSPSHTVPGMEPSNDPVLQSRLFSYPDTHR
HRLGPNYHQIPVNCPLKSGSFNPINRDGPMCVDGNLGGTPNYANAYNCPI
QYAVKPDEKYTGEVVPYHWEHTDYDYFQPKMFWKVLGRTPGEQESLVKNV
ANHVSAADEFIQDRVYEYFSKAEPIIGDLIRKKVQELKRKA
3D structure
PDB2xq1 Structural Features of Peroxisomal Catalase from the Yeast Hansenula Polymorpha
ChainG
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 G R62 V64 H65 R102 G121 V136 N138 F151 F324 V340 R344 Y348 T351 H352 R355 R59 V61 H62 R99 G118 V133 N135 F148 F321 V337 R341 Y345 T348 H349 R352
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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