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

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