1y2z Summary

pdbe.org/1y2z
spacer

T-To-T(High) quaternary transitions in human hemoglobin: betaV34G 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 2.07 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 Molecular function (GO) Biological process (GO) Cellular component (GO)
A, C (P69905) iron ion bindingsearch oxygen bindingsearch haptoglobin bindingsearch protein bindingsearch metal ion bindingsearch oxygen transporter activitysearch peroxidase activitysearch heme bindingsearch oxygen transportsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch bicarbonate transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch transportsearch cytosolsearch extracellular regionsearch hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch membranesearch
B, D (P68871) iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch peroxidase activitysearch metal ion bindingsearch hemoglobin bindingsearch haptoglobin bindingsearch oxygen transportsearch positive regulation of cell deathsearch protein heterooligomerizationsearch bicarbonate transportsearch oxidation-reduction processsearch renal absorptionsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch transportsearch response to hydrogen peroxidesearch nitric oxide transportsearch blood coagulationsearch regulation of blood vessel sizesearch platelet aggregationsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood pressuresearch extracellular vesicular exosomesearch extracellular regionsearch hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch 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