1r1x Summary

pdbe.org/1r1x
spacer

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

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