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

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