Structure of PDB 1lyc Chain A Binding Site BS01
Receptor Information
>1lyc Chain A (length=336) Species:
5346
(Coprinopsis cinerea) [
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SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDA
IGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTVEALRAVGI
NHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSSSSQPSPPSLIPGPGN
TVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF
DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACR
WQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPV
IPGGLTVDDIEVSCPSEPFPEIAAASGPLPALAPAP
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
1lyc Chain A Residue 9001 [
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Receptor-Ligand Complex Structure
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PDB
1lyc
Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase.
Resolution
1.57 Å
Binding residue
(original residue number in PDB)
S184 D201 T203 V206 D208
Binding residue
(residue number reindexed from 1)
S177 D194 T196 V199 D201
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R51 H55 H183 L200
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1lyc
,
PDBe:1lyc
,
PDBj:1lyc
PDBsum
1lyc
PubMed
12777760
UniProt
P28314
|PER_COPCI Peroxidase (Gene Name=CIP1)
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