Structure of PDB 1nqp Chain C

Receptor sequence
>1nqpC (length=141) Species: 9606 (Homo sapiens) [Search protein sequence]
VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSH
GSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKL
LSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
3D structure
PDB1nqp Crystallization and preliminary X-ray structural Studies of Hemoglobin A2 and Hemoglobin E, isolated from the blood samples of Beta-thalassemic patients
ChainC
Resolution1.73 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 C Y42 F43 F46 H58 K61 A65 L83 L86 H87 L91 N97 F98 L136 Y42 F43 F46 H58 K61 A65 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: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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nqp, PDBe:1nqp, PDBj:1nqp
PDBsum1nqp
PubMed12659864
UniProtP69905|HBA_HUMAN Hemoglobin subunit alpha (Gene Name=HBA1)

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