Structure of PDB 3l9y Chain A Binding Site BS02

Receptor Information
>3l9y Chain A (length=153) Species: 7091 (Bombyx mori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PAKAVCVLRGDVSGTVFFDQQDEKSPVVVSGEVQGLTKGKHGFHVHEFGD
NTNGCTSAGAHFNPEKQDHGGPSSAVRHVGDLGNIEAIEDAGVTKVSIQD
SQISLHGPNSIIGRTLVVHADPDDLGLGGNELSKTTGNAGGRIACGVIGL
AKI
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain3l9y Chain A Residue 156 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3l9y Crystal structures of holo and Cu-deficient Cu/Zn-SOD from the silkworm Bombyx mori and the implications in amyotrophic lateral sclerosis.
Resolution1.8 Å
Binding residue
(original residue number in PDB)
H45 H47 H120
Binding residue
(residue number reindexed from 1)
H44 H46 H119
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H45 H47 H62 H70 H79 D82 H120 R143
Catalytic site (residue number reindexed from 1) H44 H46 H61 H69 H78 D81 H119 R142
Enzyme Commision number 1.15.1.1: superoxide dismutase.
Gene Ontology
Molecular Function
GO:0004784 superoxide dismutase activity
GO:0005507 copper ion binding
GO:0008270 zinc ion binding
GO:0016209 antioxidant activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006801 superoxide metabolic process
GO:0019430 removal of superoxide radicals
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3l9y, PDBe:3l9y, PDBj:3l9y
PDBsum3l9y
PubMed20310068
UniProtP82205|SODC_BOMMO Superoxide dismutase [Cu-Zn]

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