Structure of PDB 2cah Chain A

Receptor sequence

>2cahA (length=475) Species: 584 (Proteus mirabilis)

KKLTTAAGAPVVDNNNVITAGPRGPMLLQDVWFLEKLAHFDREVIPERRM
HAKGSGAFGTFTVTHDITKYTRAKIFSEVGKKTEMFARFSTVAGERGAAD
AERDIRGFALKFYTEEGNWDMVGNNTPVFYLRDPLKFPDLNHIVKRDPRT
NMRNMAYKWDFFSHLPESLHQLTIDMSDRGLPLSYRFVHGFGSHTYSFIN
KDNERFWVKFHFRCQQGIKNLMDDEAEALVGKDRESSQRDLFEAIERGDY
PRWKLQIQIMPEKEASTVPYNPFDLTKVWPHADYPLMDVGYFELNRNPDN
YFSDVEQAAFSPANIVPGISFSPDKMLQGRLFSYGDAHRYRLGVNHHQIP
VNAPKCPFHNYHRDGAMRVDGNSGNGITYEPNSGGVFQEQPDFKEPPLSI
EGAADHWNHREDEDYFSQPRALYELLSDDEHQRMFARIAGELSQASKETQ
QRQIDLFTKVHPEYGAGVEKAIKVL

3D structure

• PDB: 2cah Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH.
• Chain: A
• Resolution: 2.7 Å

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 P137 F140 S196 F313 M329 R333 S336 Y337 H341 R344	R48 H51 R88 V122 G123 N124 P134 F137 S193 F310 M326 R330 S333 Y334 H338 R341
BS02	NDP	A	H173 S180 R182 H192 R216 V281 W282 H284 Q421 L425	H170 S177 R179 H189 R213 V278 W279 H281 Q418 L422

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

External links

• PDB: RCSB:2cah, PDBe:2cah, PDBj:2cah
• PDBsum: 2cah
• PubMed: 7791219
• UniProt: P42321|CATA_PROMI Catalase (Gene Name=katA)