Structure of PDB 1fhf Chain B Binding Site BS01
Receptor Information
>1fhf Chain B (length=304) Species:
3847
(Glycine max) [
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QLTPTFYRETCPNLFPIVFGVIFDASFTDPRIGASLMRLHFHDCFVQGCD
GSVLLNNTDTIESEQDALPNINSIRGLDVVNDIKTAVENSCPDTVSCADI
LAIAAEIASVLGGGPGWPVPLGRRDSLTANRTLANQNLPAPFFNLTQLKA
SFAVQGLNTLDLVTLSGGHTFGRARCSTFINRLYNFSNTGNPDPTLNTTY
LEVLRARCPQNATGDNLTNLDLSTPDQFDNRYYSNLLQLNGLLQSDQELF
STPGADTIPIVNSFSSNQNTFFSNFRVSMIKMGNIGVLTGDEGEIRLQCN
FVNG
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
1fhf Chain B Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
1fhf
Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
D43 V46 G48 D50 S52
Binding residue
(residue number reindexed from 1)
D43 V46 G48 D50 S52
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R38 H42 N70 H169
Catalytic site (residue number reindexed from 1)
R38 H42 N70 H169
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1fhf
,
PDBe:1fhf
,
PDBj:1fhf
PDBsum
1fhf
PubMed
11266599
UniProt
O22443
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