1hab Summary

pdbe.org/1hab
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CROSSLINKED HAEMOGLOBIN

The structure was published by Schumacher, M.A., Zheleznova, E.E., Poundstone, K.S., Kluger, R., Jones, R.T., and Brennan, R.G., in 1997 in a paper entitled "Allosteric intermediates indicate R2 is the liganded hemoglobin end state." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1996.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A.

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 heterotetramers.

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 A P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN A P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN A P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN A P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) HEMOGLOBIN A Homo sapiens
P68871 (2 - 147) HEMOGLOBIN A Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, C (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

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