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

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