Structure of PDB 1bvc Chain A Binding Site BS03

Receptor Information
>1bvc Chain A (length=153) Species: 9755 (Physeter catodon) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLK
TEAEMKASEDLKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIP
IKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELG
YQG
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1bvc Chain A Residue 158 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1bvc Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution.
Resolution1.5 Å
Binding residue
(original residue number in PDB)
H12 K16 D122
Binding residue
(residue number reindexed from 1)
H12 K16 D122
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
GO:0070062 extracellular exosome

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Biological Process

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Cellular Component
External links
PDB RCSB:1bvc, PDBe:1bvc, PDBj:1bvc
PDBsum1bvc
PubMed7707378
UniProtP02185|MYG_PHYMC Myoglobin (Gene Name=MB)

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