Structure of PDB 2frk Chain X

Receptor sequence
>2frkX (length=152) Species: 9796 (Equus caballus) [Search protein sequence]
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLK
TEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIP
IKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELG
FQ
3D structure
PDB2frk Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin.
ChainX
Resolution1.3 Å
3D
structure
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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 X T39 K42 F43 K45 H64 V68 L89 S92 H93 H97 I99 Y103 F138 T39 K42 F43 K45 H64 V68 L89 S92 H93 H97 I99 Y103 F138
BS02 NO X H64 V68 H64 V68
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:2frk, PDBe:2frk, PDBj:2frk
PDBsum2frk
PubMed16777231
UniProtP68082|MYG_HORSE Myoglobin (Gene Name=MB)

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