1ye0 Summary

pdbe.org/1ye0
spacer

T-To-T(High) quaternary transitions in human hemoglobin: betaV33A oxy (2MM IHP, 20% PEG) (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 2.5 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 hydrogen peroxide catabolic processsearch oxidation-reduction processsearch transportsearch bicarbonate transportsearch small molecule metabolic processsearch receptor-mediated endocytosissearch protein heterooligomerizationsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch oxygen bindingsearch iron ion bindingsearch heme bindingsearch protein bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch haptoglobin bindingsearch hemoglobin complexsearch extracellular regionsearch cytosolsearch membranesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch extracellular exosomesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch
B, D (P68871) oxygen transportsearch receptor-mediated endocytosissearch positive regulation of nitric oxide biosynthetic processsearch bicarbonate transportsearch nitric oxide transportsearch renal absorptionsearch transportsearch regulation of blood pressuresearch response to hydrogen peroxidesearch blood coagulationsearch positive regulation of cell deathsearch protein heterooligomerizationsearch oxidation-reduction processsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch regulation of blood vessel sizesearch platelet aggregationsearch heme bindingsearch iron ion bindingsearch oxygen bindingsearch hemoglobin bindingsearch protein bindingsearch oxygen transporter activitysearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch extracellular exosomesearch hemoglobin complexsearch extracellular regionsearch cytosolsearch 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