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

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