1nqp Summary

pdbe.org/1nqp
spacer

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

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