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