Structure of PDB 2nrl Chain A

Receptor sequence
>2nrlA (length=145) Species: 48168 (Thunnus atlanticus) [Search protein sequence]
ADFDAVLKCWGPVEADYTTIGGLVLTRLFKEHPETQKLFPKFAGIAQADI
AGNAAVSAHGATVLKKLGELLKAKGSHAAILKPLANSHATKHKIPINNFK
LISEVLVKVMQEKAGLDAGGQTALRNVMGIIIADLEANYKELGFS
3D structure
PDB2nrl S-nitrosylation-induced conformational change in blackfin tuna myoglobin.
ChainA
Resolution0.91 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 1.11.1.-
1.7.-.-
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 L39 F40 K42 H60 V64 L85 S88 H89 H93 I95 N99 F100 L38 F39 K41 H59 V63 L84 S87 H88 H92 I94 N98 F99
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2nrl, PDBe:2nrl, PDBj:2nrl
PDBsum2nrl
PubMed17488722
UniProtP68190|MYG_THUOR Myoglobin (Gene Name=mb)

[Back to BioLiP]