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

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