Structure of PDB 1myg Chain A Binding Site BS01

Receptor Information
>1myg Chain A (length=153) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETLEKFDKFKHLK
SEDEMKASEDLKKHGNTVLTALGGILKKKGHHEAELTPLAQSHATKHKIP
VKYLEFISEAIIQVLQSKHPGDFGADAQGAMSKALELFRNDMAAKYKELG
FQG
Ligand information
Ligand IDSO4
InChIInChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKeyQAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)[O-]
CACTVS 3.341[O-][S]([O-])(=O)=O
ACDLabs 10.04[O-]S([O-])(=O)=O
FormulaO4 S
NameSULFATE ION
ChEMBL
DrugBankDB14546
ZINC
PDB chain1myg Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1myg High-resolution X-ray structures of pig metmyoglobin and two CD3 mutants: Mb(Lys45----Arg) and Mb(Lys45----Ser).
Resolution1.75 Å
Binding residue
(original residue number in PDB)
K63 H64 T67
Binding residue
(residue number reindexed from 1)
K63 H64 T67
Annotation score1
Enzymatic activity
Enzyme Commision number 1.11.1.-
1.7.-.-
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0005344 oxygen carrier activity
GO:0016491 oxidoreductase activity
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0098809 nitrite reductase activity
Biological Process
GO:0015671 oxygen transport
GO:0019430 removal of superoxide radicals
Cellular Component
GO:0005737 cytoplasm
GO:0016528 sarcoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1myg, PDBe:1myg, PDBj:1myg
PDBsum1myg
PubMed1390659
UniProtP02189|MYG_PIG Myoglobin (Gene Name=MB)

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