Structure of PDB 1y85 Chain D

Receptor sequence
>1y85D (length=145) Species: 9606 (Homo sapiens) [Search protein sequence]
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLST
PDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDP
ENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKY
3D structure
PDB1y85 Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions.
ChainD
Resolution2.13 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 D F41 F42 H63 K66 V67 L88 H92 L96 N102 F103 L141 F41 F42 H63 K66 V67 L88 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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1y85, PDBe:1y85, PDBj:1y85
PDBsum1y85
PubMed15835899
UniProtP68871|HBB_HUMAN Hemoglobin subunit beta (Gene Name=HBB)

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