Structure of PDB 5ker Chain A

Receptor sequence
>5kerA (length=140) Species: 10042 (Peromyscus maniculatus) [Search protein sequence]
VLSADDKANIKAAWGKIGGHGAEYGAEALERMFCSFPTTKTYFPHFDVSP
GSAQVKGHGAKVAGALATAASHLDDLPAALSALSDLHAHKLRVDPVNFKL
LSHCLLVTLAAHHPAEFTPAVHASLDKFLASVSTVLTSKY
3D structure
PDB5ker Alteration of the alpha 1 beta 2/ alpha 2 beta 1 subunit interface contributes to the increased hemoglobin-oxygen affinity of high-altitude deer mice.
ChainA
Resolution2.202 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 A Y42 F43 H45 F46 H58 K61 V62 L83 L86 H87 L91 N97 F98 L136 Y42 F43 H45 F46 H58 K61 V62 L83 L86 H87 L91 N97 F98 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
GO:0072562 blood microparticle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ker, PDBe:5ker, PDBj:5ker
PDBsum5ker
PubMed28362841
UniProtA4ZQ87

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