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

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