1hac Summary

pdbe.org/1hac
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 2.6 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) Cellular component (GO) Molecular function (GO)
A, C (P69905) small molecule metabolic processsearch bicarbonate transportsearch response to hydrogen peroxidesearch oxygen transportsearch hydrogen peroxide catabolic processsearch transportsearch oxidation-reduction processsearch positive regulation of cell deathsearch protein heterooligomerizationsearch extracellular vesicular exosomesearch membranesearch extracellular regionsearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch cytosolsearch blood microparticlesearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch metal ion bindingsearch oxygen bindingsearch peroxidase activitysearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch heme bindingsearch iron ion bindingsearch
B, D (P68871) bicarbonate transportsearch platelet aggregationsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch regulation of blood vessel sizesearch transportsearch oxygen transportsearch renal absorptionsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch small molecule metabolic processsearch blood coagulationsearch nitric oxide transportsearch oxidation-reduction processsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood pressuresearch extracellular regionsearch hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch heme bindingsearch protein bindingsearch oxygen bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch peroxidase activitysearch iron ion bindingsearch

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