Structure of PDB 1arv Chain A Binding Site BS01
Receptor Information
>1arv 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 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
1arv Chain A Residue 346 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1arv
Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis.
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
D57 G75 D77 S79
Binding residue
(residue number reindexed from 1)
D49 G67 D69 S71
Annotation score
1
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1arv
,
PDBe:1arv
,
PDBj:1arv
PDBsum
1arv
PubMed
7665612
UniProt
P28313
|PER_ARTRA Peroxidase
[
Back to BioLiP
]