Structure of PDB 1ck6 Chain A Binding Site BS02

Receptor Information
>1ck6 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 chain1ck6 Chain A Residue 346 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ck6 Binding of salicylhydroxamic acid and several aromatic donor molecules to Arthromyces ramosus peroxidase, investigated by X-ray crystallography, optical difference spectroscopy, NMR relaxation, molecular dynamics, and kinetics.
Resolution1.9 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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Biological Process
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Cellular Component
External links
PDB RCSB:1ck6, PDBe:1ck6, PDBj:1ck6
PDBsum1ck6
PubMed10504224
UniProtP28313|PER_ARTRA Peroxidase

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