Structure of PDB 1m85 Chain A

Receptor sequence
>1m85A (length=476) Species: 584 (Proteus mirabilis) [Search protein sequence]
KKLTTAAGAPVVDNNNVITAGPRGPMLLQDVWFLEKLAHFDREVIPERRM
HAKGSGAFGTFTVTHDITKYTRAKIFSEVGKKTEMFARFSTVAGERGAAD
AERDIRGFALKFYTEEGNWDMVGNNTPVFYLRDPLKFPDLNHIVKRDPRT
NMRNMAYKWDFFSHLPESLHQLTIDMSDRGLPLSYRFVHGFGSHTYSFIN
KDNERFWVKFHFRCQQGIKNLMDDEAEALVGKDRESSQRDLFEAIERGDY
PRWKLQIQIMPEKEASTVPYNPFDLTKVWPHADYPLMDVGYFELNRNPDN
YFSDVEQAAFSPANIVPGISFSPDKMLQGRLFSYGDAHRYRLGVNHHQIP
VNAPKCPFHNYHRDGAMRVDGNSGNGITYEPNSGGVFQEQPDFKEPPLSI
EGAADHWNHREDEDYFSQPRALYELLSDDEHQRMFARIAGELSQASKETQ
QRQIDLFTKVHPEYGAGVEKAIKVLE
3D structure
PDB1m85 Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH.
ChainA
Resolution2.0 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 HEM A R51 H54 R91 V125 G126 N127 F140 S196 F313 M329 R333 S336 Y337 H341 R344 R48 H51 R88 V122 G123 N124 F137 S193 F310 M326 R330 S333 Y334 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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Cellular Component
External links
PDB RCSB:1m85, PDBe:1m85, PDBj:1m85
PDBsum1m85
PubMed7791219
UniProtP42321|CATA_PROMI Catalase (Gene Name=katA)

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