1abw Summary

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DEOXY 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 2.0 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-BASED BLOOD SUBSTITUTE.

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-BASED BLOOD SUBSTITUTE P69905 (1-142) (HBA_HUMAN)search Homo sapienssearch 98% 283 100%
B HEMOGLOBIN-BASED BLOOD SUBSTITUTE P68871 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN-BASED BLOOD SUBSTITUTE 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-BASED BLOOD SUBSTITUTE Homo sapiens
P68871 (3 - 147) HEMOGLOBIN-BASED BLOOD SUBSTITUTE 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) heme bindingsearch iron ion bindingsearch protein bindingsearch haptoglobin bindingsearch metal ion bindingsearch oxygen transporter activitysearch peroxidase activitysearch oxygen bindingsearch oxygen transportsearch oxidation-reduction processsearch receptor-mediated endocytosissearch small molecule metabolic processsearch bicarbonate transportsearch transportsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch positive regulation of cell deathsearch hemoglobin complexsearch cytosolic small ribosomal subunitsearch extracellular regionsearch haptoglobin-hemoglobin complexsearch cytosolsearch extracellular vesicular exosomesearch membranesearch blood microparticlesearch endocytic vesicle lumensearch
B, D (P68871) iron ion bindingsearch heme bindingsearch protein bindingsearch oxygen transporter activitysearch metal ion bindingsearch oxygen bindingsearch hemoglobin bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transportsearch blood coagulationsearch bicarbonate transportsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch regulation of blood pressuresearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch platelet aggregationsearch transportsearch renal absorptionsearch small molecule metabolic processsearch nitric oxide transportsearch oxidation-reduction processsearch regulation of blood vessel sizesearch receptor-mediated endocytosissearch positive regulation of nitric oxide biosynthetic processsearch haptoglobin-hemoglobin complexsearch extracellular regionsearch cytosolsearch hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch endocytic vesicle lumensearch

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