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