1r1y Summary

pdbe.org/1r1y
spacer

Crystal structure of deoxy-human hemoglobin Bassett at 1.8 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 1.8 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%
C 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%
D 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, C (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

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