1y0t Summary

pdbe.org/1y0t
spacer

T-to-T(High) Quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (1 test set)

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

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