Structure of PDB 2e3b Chain A

Receptor sequence
>2e3bA (length=336) Species: 5451 (Agaricales sp. 'Arthromyces ramosus') [Search protein sequence]
SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDA
IGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTIEALRAVGI
NHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGN
TVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF
DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACR
WQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPV
IPGGLTVDDIEVSCPSEPFPEIATASGPLPSLAPAP
3D structure
PDB2e3b Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosusperoxidase at 100 K refined to 1.3 A resolution: coordination geometries of the ligands to the haem iron
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R52 H56 H184 L201
Catalytic site (residue number reindexed from 1) R44 H48 H176 L193
Enzyme Commision number 1.11.1.7: peroxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0140825 lactoperoxidase activity
Biological Process
GO:0000302 response to reactive oxygen species
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress
GO:0042744 hydrogen peroxide catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region

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Molecular Function

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Cellular Component
External links
PDB RCSB:2e3b, PDBe:2e3b, PDBj:2e3b
PDBsum2e3b
PubMed17372351
UniProtP28313|PER_ARTRA Peroxidase

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