Structure of PDB 1fhf Chain C

Receptor sequence
>1fhfC (length=304) Species: 3847 (Glycine max) [Search protein sequence]
QLTPTFYRETCPNLFPIVFGVIFDASFTDPRIGASLMRLHFHDCFVQGCD
GSVLLNNTDTIESEQDALPNINSIRGLDVVNDIKTAVENSCPDTVSCADI
LAIAAEIASVLGGGPGWPVPLGRRDSLTANRTLANQNLPAPFFNLTQLKA
SFAVQGLNTLDLVTLSGGHTFGRARCSTFINRLYNFSNTGNPDPTLNTTY
LEVLRARCPQNATGDNLTNLDLSTPDQFDNRYYSNLLQLNGLLQSDQELF
STPGADTIPIVNSFSSNQNTFFSNFRVSMIKMGNIGVLTGDEGEIRLQCN
FVNG
3D structure
PDB1fhf Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions.
ChainC
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA C D43 V46 G48 D50 S52 D43 V46 G48 D50 S52
BS02 CA C T170 D221 T224 Q227 D229 T170 D221 T224 Q227 D229
BS03 HEM C R31 A34 S35 R38 F41 S73 F152 L165 H169 G172 R173 A174 R175 R31 A34 S35 R38 F41 S73 F152 L165 H169 G172 R173 A174 R175
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:1fhf, PDBe:1fhf, PDBj:1fhf
PDBsum1fhf
PubMed11266599
UniProtO22443

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