Structure of PDB 5ker Chain G

Receptor sequence
>5kerG (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.
ChainG
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 G Y42 F43 H45 H58 K61 L83 H87 L91 N97 F98 L101 L136 Y42 F43 H45 H58 K61 L83 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
GO:0072562 blood microparticle

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Cellular Component
External links
PDB RCSB:5ker, PDBe:5ker, PDBj:5ker
PDBsum5ker
PubMed28362841
UniProtA4ZQ87

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