1y4q Summary

pdbe.org/1y4q
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T-To-T(High) quaternary transitions in human hemoglobin: betaF42A 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 2.11 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 transportsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch protein heterooligomerizationsearch small molecule metabolic processsearch protein bindingsearch iron ion bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch heme bindingsearch haptoglobin bindingsearch oxygen bindingsearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch cytosolsearch blood microparticlesearch cytosolic small ribosomal subunitsearch membranesearch
B, D (P68871) transportsearch regulation of blood vessel sizesearch renal absorptionsearch nitric oxide transportsearch protein heterooligomerizationsearch bicarbonate transportsearch response to hydrogen peroxidesearch platelet aggregationsearch oxygen transportsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch positive regulation of nitric oxide biosynthetic processsearch oxidation-reduction processsearch regulation of blood pressuresearch blood coagulationsearch small molecule metabolic processsearch protein bindingsearch hemoglobin bindingsearch oxygen transporter activitysearch oxygen bindingsearch heme bindingsearch iron ion bindingsearch haptoglobin bindingsearch peroxidase activitysearch metal ion bindingsearch extracellular regionsearch cytosolsearch hemoglobin complexsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch blood microparticlesearch

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