1aby Summary

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CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)

The structure was published by Kroeger, K.S. and Kundrot, C.E., in 1997 in a paper entitled "Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN.

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 heterotrimers.

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 P69905 (1-142) (HBA_HUMAN)search Homo sapienssearch 98% 283 100%
B HEMOGLOBIN P68871 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN P68871 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (1 - 142) HEMOGLOBIN Homo sapiens
P68871 (3 - 147) HEMOGLOBIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

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