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

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