Structure of PDB 1atj Chain D Binding Site BS01
Receptor Information
>1atj Chain D (length=306) Species:
3704
(Armoracia rusticana) [
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QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCD
ASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSCADL
LTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKD
SFRNVGLNRSSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTT
YLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQKGLIQSDQEL
FSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLN
CRVVNS
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
1atj Chain D Residue 351 [
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Receptor-Ligand Complex Structure
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PDB
1atj
Crystal structure of horseradish peroxidase C at 2.15 A resolution.
Resolution
2.15 Å
Binding residue
(original residue number in PDB)
T171 D222 T225 I228 D230
Binding residue
(residue number reindexed from 1)
T171 D222 T225 I228 D230
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R38 H42 N70 H170
Catalytic site (residue number reindexed from 1)
R38 H42 N70 H170
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:0006979
response to oxidative stress
GO:0042744
hydrogen peroxide catabolic process
GO:0098869
cellular oxidant detoxification
Cellular Component
GO:0005576
extracellular region
GO:0005773
vacuole
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1atj
,
PDBe:1atj
,
PDBj:1atj
PDBsum
1atj
PubMed
9406554
UniProt
P00433
|PER1A_ARMRU Peroxidase C1A (Gene Name=PRXC1A)
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