Structure of PDB 2e3b Chain A Binding Site BS02

Receptor Information
>2e3b Chain A (length=336) Species: 5451 (Agaricales sp. 'Arthromyces ramosus') [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDA
IGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTIEALRAVGI
NHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGN
TVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF
DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACR
WQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPV
IPGGLTVDDIEVSCPSEPFPEIATASGPLPSLAPAP
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2e3b Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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
Resolution1.3 Å
Binding residue
(original residue number in PDB)		D57 G75 D77 S79
Binding residue
(residue number reindexed from 1)		D49 G67 D69 S71
Annotation score1
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.
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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Cellular Component
External links
PDB RCSB:2e3b, PDBe:2e3b, PDBj:2e3b
PDBsum2e3b
PubMed17372351
UniProtP28313|PER_ARTRA Peroxidase

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