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

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