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