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