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

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