Structure of PDB 3hf4 Chain F

Receptor sequence
>3hf4F (length=146) Species: 10116 (Rattus norvegicus) [Search protein sequence]
VHLTDAEKAAVNGLWGKVNPDDVGGEALGRLLVVYPWTQRYFDSFGDLSS
ASAIMGNPKVKAHGKKVINAFNDGLKHLDNLKGTFAHLSELHCDKLHVDP
ENFRLLGNMIVIVLGHHLGKEFTPCAQAAFQKVVAGVASALAHKYH
3D structure
PDB3hf4 Quaternary structural variability in rat hemoglobin
ChainF
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 F Y41 F42 H63 K66 V67 L88 H92 L96 V98 N102 F103 L106 L141 Y41 F42 H63 K66 V67 L88 H92 L96 V98 N102 F103 L106 L141
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0005344 oxygen carrier activity
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0030492 hemoglobin binding
GO:0031720 haptoglobin binding
GO:0031721 hemoglobin alpha binding
GO:0031722 hemoglobin beta binding
GO:0043177 organic acid binding
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0015670 carbon dioxide transport
GO:0015671 oxygen transport
GO:0030097 hemopoiesis
GO:0030185 nitric oxide transport
GO:0042542 response to hydrogen peroxide
GO:0042744 hydrogen peroxide catabolic process
GO:0048821 erythrocyte development
GO:0070293 renal absorption
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005615 extracellular space
GO:0005833 hemoglobin complex
GO:0031838 haptoglobin-hemoglobin complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3hf4, PDBe:3hf4, PDBj:3hf4
PDBsum3hf4
PubMed
UniProtP02091|HBB1_RAT Hemoglobin subunit beta-1 (Gene Name=Hbb)

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