Structure of PDB 2isa Chain H

Receptor sequence
>2isaH (length=482) Species: 316275 (Aliivibrio salmonicida LFI1238) [Search protein sequence]
SKKLTTAAGCPVAHNQNVQTAGKRGPQLLQDVWFLEKLAHFDREVIPERR
MHAKGSGAYGTFTVTHDITKYTKAKIFSDIGKKTDMFARFSTVAGERGAA
DAERDIRGFSLKFYTEEGNWDLAGNNTPVFFLRDPLKFPDLNHAVKRDPR
TNMRSAKNNWDFWTSLPEALHQVTIVMSDRGIPATYRHMHGFGSHTFSFI
NSDNERYWVKFHFVSQQGIKNLSDAEAGELVGNDRESHQRDLLDSIDNQD
FPKWTLKVQIMPEADAATVPYNPFDLTKVWPHKDYPLIEVGEFELNRNPQ
NYFAEVEQAAFNPANVVPGISFSPDKMLQGRLFAYGDAQRYRLGVNHQHI
PVNAPRCPVHSYHRDGAMRVDGNFGSTLGYEPNDQGQWAEQPDFSEPPLN
LDGAAAHWDHREDEDYFSQPGDLFGLMTAEKQAILFDNTARNLNGVPKEI
QLRHVTHCYKADPAYGEGIGKLLGFDISEYNS
3D structure
PDB2isa The first structure of a cold-active catalase from Vibrio salmonicida at 1.96A reveals structural aspects of cold adaptation
ChainH
Resolution1.97 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 N314
Catalytic site (residue number reindexed from 1) H52 N125 N312
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 H R51 H54 R91 S112 A125 G126 N127 P137 F140 S196 F313 M329 R333 Y337 Q341 R344 R49 H52 R89 S110 A123 G124 N125 P135 F138 S194 F311 M327 R331 Y335 Q339 R342
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:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2isa, PDBe:2isa, PDBj:2isa
PDBsum2isa
PubMed17242507
UniProtQ3LSM1

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