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

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