1hab Summary

pdbe.org/1hab
spacer

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

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