Structure of PDB 1o1p Chain B

Receptor sequence

>1o1pB (length=146) Species: 9606 (Homo sapiens)

MHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLST
PDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHADKLHVDP
ENFRLLGKVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH

3D structure

• PDB: 1o1p A Human Recombinant Hemoglobin Designed for Use as a Blood Substitute
• Chain: B
• Resolution: 1.8 Å

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	B	F41 F42 H63 K66 V67 A70 H92 L96 N102 F103 L141	F41 F42 H63 K66 V67 A70 H92 L96 N102 F103 L141

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0005344 oxygen carrier activity
• GO:0005515 protein binding
• GO:0019825 oxygen binding
• GO:0020037 heme binding
• GO:0030492 hemoglobin binding
• GO:0031720 haptoglobin binding
• GO:0031721 hemoglobin alpha binding
• GO:0043177 organic acid binding
• GO:0046872 metal ion binding

Biological Process

• GO:0008217 regulation of blood pressure
• GO:0015670 carbon dioxide transport
• GO:0015671 oxygen transport
• GO:0030185 nitric oxide transport
• GO:0042542 response to hydrogen peroxide
• GO:0042744 hydrogen peroxide catabolic process
• GO:0045429 positive regulation of nitric oxide biosynthetic process
• GO:0070293 renal absorption
• GO:0070527 platelet aggregation
• GO:0097746 blood vessel diameter maintenance
• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0005829 cytosol
• GO:0005833 hemoglobin complex
• GO:0031838 haptoglobin-hemoglobin complex
• GO:0070062 extracellular exosome
• GO:0071682 endocytic vesicle lumen
• GO:0072562 blood microparticle
• GO:1904724 tertiary granule lumen
• GO:1904813 ficolin-1-rich granule lumen

External links

• PDB: RCSB:1o1p, PDBe:1o1p, PDBj:1o1p
• PDBsum: 1o1p
• UniProt: P68871|HBB_HUMAN Hemoglobin subunit beta (Gene Name=HBB)