1y45 Summary

pdbe.org/1y45
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T-To-T(high) quaternary transitions in human hemoglobin: betaP36A deoxy low-salt (10 test sets)

The structure was published by Kavanaugh, J.S., Rogers, P.H., and Arnone, A., in 2005 in a paper entitled "Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2004.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Hemoglobin alpha chain and Hemoglobin beta chain.

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 alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D Hemoglobin beta chain 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 alpha chain Homo sapiens
P68871 (2 - 147) Hemoglobin beta chain 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 oxidation-reduction processsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch protein heterooligomerizationsearch small molecule metabolic processsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch receptor-mediated endocytosissearch transportsearch heme bindingsearch oxygen bindingsearch iron ion bindingsearch peroxidase activitysearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch hemoglobin complexsearch endocytic vesicle lumensearch extracellular regionsearch extracellular exosomesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch cytosolsearch membranesearch cytosolic small ribosomal subunitsearch
B, D (P68871) oxygen transportsearch oxidation-reduction processsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood vessel sizesearch receptor-mediated endocytosissearch bicarbonate transportsearch small molecule metabolic processsearch nitric oxide transportsearch renal absorptionsearch transportsearch regulation of blood pressuresearch hydrogen peroxide catabolic processsearch platelet aggregationsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch blood coagulationsearch protein heterooligomerizationsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch peroxidase activitysearch hemoglobin bindingsearch metal ion bindingsearch heme bindingsearch oxygen transporter activitysearch hemoglobin complexsearch cytosolsearch extracellular exosomesearch extracellular regionsearch haptoglobin-hemoglobin complexsearch 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