1nqp Summary

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Crystal structure of Human hemoglobin E at 1.73 A resolution

The structure was published by Dasgupta, J., Sen, U., Choudhury, D., et al., Chakrabarty, S.B., Chakrabarty, A., and Dattagupta, J.K., in 2004 in a paper entitled "Crystallization and preliminary X-ray structural Studies of Hemoglobin A2 and Hemoglobin E, isolated from the blood samples of Beta-thalassemic patients" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.73 Å and deposited in 2003.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Hemoglobin alpha chain and Hemoglobin beta chain.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms heterotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) Hemoglobin alpha chain Homo sapiens
P68871 (2 - 147) Hemoglobin beta chain Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, C (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, C (P69905) iron ion bindingsearch oxygen bindingsearch heme bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transportsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch protein heterooligomerizationsearch transportsearch small molecule metabolic processsearch oxidation-reduction processsearch positive regulation of cell deathsearch membranesearch extracellular regionsearch hemoglobin complexsearch extracellular vesicular exosomesearch cytosolsearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch endocytic vesicle lumensearch
B, D (P68871) oxygen bindingsearch heme bindingsearch protein bindingsearch haptoglobin bindingsearch hemoglobin bindingsearch oxygen transporter activitysearch metal ion bindingsearch iron ion bindingsearch peroxidase activitysearch oxygen transportsearch regulation of blood pressuresearch regulation of blood vessel sizesearch protein heterooligomerizationsearch nitric oxide transportsearch positive regulation of cell deathsearch transportsearch hydrogen peroxide catabolic processsearch renal absorptionsearch bicarbonate transportsearch platelet aggregationsearch oxidation-reduction processsearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch response to hydrogen peroxidesearch small molecule metabolic processsearch hemoglobin complexsearch cytosolsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch endocytic vesicle lumensearch blood microparticlesearch

Chain InterPro annotation
A, C Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
B, D Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch