1hac Summary

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

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