1bbb Summary

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A THIRD QUATERNARY STRUCTURE OF HUMAN HEMOGLOBIN A AT 1.7-ANGSTROMS RESOLUTION

The structure was published by Silva, M.M., Rogers, P.H., and Arnone, A., in 1992 in a paper entitled "A third quaternary structure of human hemoglobin A at 1.7-A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1992.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A (CARBONMONOXY) (ALPHA CHAIN) and HEMOGLOBIN A (CARBONMONOXY) (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 A (CARBONMONOXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN A (CARBONMONOXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN A (CARBONMONOXY) (BETA CHAIN) P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN A (CARBONMONOXY) (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 A (CARBONMONOXY) (ALPHA CHAIN) Homo sapiens
P68871 (2 - 147) HEMOGLOBIN A (CARBONMONOXY) (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 Molecular function (GO) Cellular component (GO) Biological process (GO)
A, C (P69905) iron ion bindingsearch oxygen bindingsearch protein bindingsearch heme bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch metal ion bindingsearch peroxidase activitysearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch blood microparticlesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch cytosolsearch membranesearch oxidation-reduction processsearch small molecule metabolic processsearch oxygen transportsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch transportsearch response to hydrogen peroxidesearch bicarbonate transportsearch positive regulation of cell deathsearch
B, D (P68871) protein bindingsearch oxygen transporter activitysearch heme bindingsearch haptoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen bindingsearch hemoglobin bindingsearch iron ion bindingsearch extracellular regionsearch cytosolsearch hemoglobin complexsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch bicarbonate transportsearch oxygen transportsearch protein heterooligomerizationsearch positive regulation of cell deathsearch platelet aggregationsearch response to hydrogen peroxidesearch small molecule metabolic processsearch renal absorptionsearch regulation of blood vessel sizesearch positive regulation of nitric oxide biosynthetic processsearch blood coagulationsearch nitric oxide transportsearch transportsearch oxidation-reduction processsearch hydrogen peroxide catabolic processsearch regulation of blood pressuresearch

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