Structure of PDB 2j2m Chain D

Receptor sequence
>2j2mD (length=480) Species: 223958 (Exiguobacterium oxidotolerans) [Search protein sequence]
KKLTTNQGVPIGDNQNSRTAGRRGPTLLEDYQLIEKIAHFDRERVPERVV
HARGFGAHGVFKVKNSMKKYTKAAFLQEEGTEVPVFARFSTVIHGTHSPE
TLRDPRGFSVKFYTEEGNWDFVGNNLPVFFIRDAMKFPDMVHSLKPDPRT
NIQDPDRYWDFMTLRPESTNMLMHIFTDEGIPASYRKMRGSSVHSFKWVN
AHGNTVYIKLRWVPKEGVHNLSADEATEVQGKDFNHASNDTFQAIENGDF
PEWDLFVQVLDPADVENFDFDPLDATKDWFEDVIPFQHVGTMTLNKNVDN
YFAETESVGFNPGVLVPGMLPSEDKLLQGRLFSYSDTQRHRIGPNYQQLP
INCPFAQVNNYQRDGAMPFKQQTSSVNYEPNRYQDEPKQTPEYTEDTQPL
HDDIHGRLEIEKTNNFGQAGEVYRRMTEEEQMALLNNLVNDLQQVRHENT
VLLAICNFYRADASLGEKLSEALNVDIKPF
3D structure
PDB2j2m Relationship between the Size of the Bottleneck 15 a from Iron in the Main Channel and the Reactivity of Catalase Corresponding to the Molecular Size of Substrates.
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H56 N129 N316
Catalytic site (residue number reindexed from 1) H51 N124 N311
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 D R53 V55 H56 R93 S114 V127 G128 N129 F134 F142 V198 H199 F315 L331 G334 R335 S338 Y339 T342 Q343 R346 R48 V50 H51 R88 S109 V122 G123 N124 F129 F137 V193 H194 F310 L326 G329 R330 S333 Y334 T337 Q338 R341
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
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:2j2m, PDBe:2j2m, PDBj:2j2m
PDBsum2j2m
PubMed17198371
UniProtA2A136

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