Structure of PDB 3ia3 Chain B

Receptor sequence
>3ia3B (length=135) Species: 9606 (Homo sapiens) [Search protein sequence]
LSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHG
SAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLL
SHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVL
3D structure
PDB3ia3 A cis-proline in alpha-hemoglobin stabilizing protein directs the structural reorganization of alpha-hemoglobin.
ChainB
Resolution3.2 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 B F43 H45 F46 H58 K61 V62 L83 H87 L91 V93 N97 F98 L101 S102 F42 H44 F45 H57 K60 V61 L82 H86 L90 V92 N96 F97 L100 S101
BS02 HEM B M76 P77 N78 M75 P76 N77
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0005344 oxygen carrier activity
GO:0005506 iron ion binding
GO:0005515 protein 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: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:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005829 cytosol
GO:0005833 hemoglobin complex
GO:0016020 membrane
GO:0031838 haptoglobin-hemoglobin complex
GO:0070062 extracellular exosome
GO:0071682 endocytic vesicle lumen
GO:0072562 blood microparticle

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Biological Process

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Cellular Component
External links
PDB RCSB:3ia3, PDBe:3ia3, PDBj:3ia3
PDBsum3ia3
PubMed19706593
UniProtP69905|HBA_HUMAN Hemoglobin subunit alpha (Gene Name=HBA1)

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