Structure of PDB 3pel Chain A

Receptor sequence

>3pelA (length=141) Species: 9615 (Canis lupus familiaris)

VLSPADKTNIKSTWDKIGGHAGDYGGEALDRTFQSFPTTKTYFPHFDLSP
GSAQVKAHGKKVADALTTAVAHLDDLPGALSALSDLHAYKLRVDPVNFKL
LSHCLLVTLACHHPTEFTPAVHASLDKFFAAVSTVLTSKYR

3D structure

• PDB: 3pel Structure of Greyhound hemoglobin: origin of high oxygen affinity.
• Chain: A
• 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	A	Y42 F43 H45 F46 H58 K61 A65 L83 L86 H87 L91 N97 F98 L101 L136	Y42 F43 H45 F46 H58 K61 A65 L83 L86 H87 L91 N97 F98 L101 L136

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0005344 oxygen carrier activity
• GO:0005506 iron ion binding
• GO:0019825 oxygen binding
• GO:0020037 heme binding
• GO:0031720 haptoglobin 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: P60529|HBA_CANLF Hemoglobin subunit alpha (Gene Name=HBA)