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

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