Structure of PDB 1si8 Chain C

Receptor sequence
>1si8C (length=474) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
QHLTTSQGSPVGDNQNSLTAGEFGPVLIQDVHLLEKLAHFNRERVPERVV
HAKGAGAHGIFKVSQSMAQYTKADFLSEVGKETPLFARFSTVAGELGSSD
TLRDPRGFALKFYTDEGNYDLVGNNTPIFFIRDAIKFPDFIHSQKRNPRT
HLKSPEAVWDFWSHSPESLHQVTILMSDRGIPLSFRHMHGFGSHTFKWVN
AAGEVFFVKYHFKTNQGIKNLESQLAEEIAGKNPDFHIEDLHNAIENQEF
PSWTLSVQIIPYADALTMKETLFDVTKTVSQKEYPLIEVGTMTLNRNPEN
YFAEVEQVTFSPGNFVPGIEASPDKLLQGRLFAYGDAHRHRVGANSHQLP
INQAKAPVNNYQKDGNMRFNNGNSEINYEPNSYTETPKEDPTAKISSFEV
EGNVGNYSYNQDHFTQANALYNLLPSEEKENLINNIAASLGQVKNQEIIA
RQIDLFTRVNPEYGARVAQAIKQQ
3D structure
PDB1si8 The three-dimensional structure of catalase from Enterococcus faecalis.
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H54 N127 S314
Catalytic site (residue number reindexed from 1) H51 N124 S311
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 SO4 C R182 H192 R179 H189
BS02 HEM C R51 V53 H54 R91 V125 G126 N127 F132 A137 F140 S196 F313 L329 R333 Y337 A340 H341 R344 R48 V50 H51 R88 V122 G123 N124 F129 A134 F137 S193 F310 L326 R330 Y334 A337 H338 R341
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1si8, PDBe:1si8, PDBj:1si8
PDBsum1si8
PubMed15272159
UniProtQ834P5

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