1r1x Summary

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Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom

The structure was published by Abdulmalik, O., Safo, M.K., Lerner, N.B., et al., Santacroce, R., Abraham, D.J., and Asakura, T., in 2004 in a paper entitled "Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.15 Å and deposited in 2003.

The experimental data on which the structure is based was also 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%
B 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 (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

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