Structure of PDB 3pel Chain B

Receptor sequence

>3pelB (length=146) Species: 9615 (Canis lupus familiaris)

VHLTAEEKSLVSGLWGKVNVDEVGGEALGRLLIVYPWTQRFFDSFGDLST
PDAVMSNAKVKAHGKKVLNSFSDGLKNLDNLKGTFAKLSELHCDKLHVDP
ENFKLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH

3D structure

• PDB: 3pel Structure of Greyhound hemoglobin: origin of high oxygen affinity.
• Chain: B
• Resolution: 1.9 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	T38 F41 F42 H63 S70 F71 L88 H92 L96 V98 N102 F103 L106 L141	T38 F41 F42 H63 S70 F71 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:0031720 haptoglobin binding
• GO:0031721 hemoglobin alpha binding
• GO:0043177 organic acid binding
• GO:0046872 metal ion binding

Biological Process

• GO:0015671 oxygen transport
• GO:0042744 hydrogen peroxide catabolic process
• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0005833 hemoglobin complex
• GO:0031838 haptoglobin-hemoglobin complex

External links

• PDB: RCSB:3pel, PDBe:3pel, PDBj:3pel
• PDBsum: 3pel
• PubMed: 21543841
• UniProt: P60524|HBB_CANLF Hemoglobin subunit beta (Gene Name=HBB)