Structure of PDB 5l86 Chain A

Receptor sequence
>5l86A (length=247) Species: 3847 (Glycine max) [Search protein sequence]
KSYPTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTK
TGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFPILSYADFYQLAGV
VAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKAMGLT
DQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGL
LQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGFAD
3D structure
PDB5l86 A Chemically Programmed Proximal Ligand Enhances the Catalytic Properties of a Heme Enzyme.
ChainA
Resolution1.9 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 L66 H163 W179 D208
Catalytic site (residue number reindexed from 1) R36 H40 L64 H161 W177 D206
Enzyme Commision number 1.11.1.11: L-ascorbate 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 HEM A P34 L37 R38 F41 P132 P134 F145 L159 H163 G166 A167 A168 H169 R172 S173 W179 P32 L35 R36 F39 P130 P132 F143 L157 H161 G164 A165 A166 H167 R170 S171 W177
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016688 L-ascorbate peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress
GO:0098869 cellular oxidant detoxification

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Molecular Function
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Biological Process
External links
PDB RCSB:5l86, PDBe:5l86, PDBj:5l86
PDBsum5l86
PubMed27500802
UniProtQ43758

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