1ye2 Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaY35F 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 1.8 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 Cellular component (GO) Molecular function (GO) Biological process (GO)
A, C (P69905) hemoglobin complexsearch cytosolsearch blood microparticlesearch extracellular regionsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch membranesearch cytosolic small ribosomal subunitsearch heme bindingsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch haptoglobin bindingsearch bicarbonate transportsearch oxidation-reduction processsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch transportsearch small molecule metabolic processsearch protein heterooligomerizationsearch positive regulation of cell deathsearch oxygen transportsearch
B, D (P68871) haptoglobin-hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch blood microparticlesearch heme bindingsearch metal ion bindingsearch peroxidase activitysearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch hemoglobin bindingsearch oxygen bindingsearch iron ion bindingsearch oxidation-reduction processsearch oxygen transportsearch small molecule metabolic processsearch blood coagulationsearch response to hydrogen peroxidesearch regulation of blood vessel sizesearch positive regulation of nitric oxide biosynthetic processsearch platelet aggregationsearch transportsearch bicarbonate transportsearch hydrogen peroxide catabolic processsearch renal absorptionsearch positive regulation of cell deathsearch regulation of blood pressuresearch protein heterooligomerizationsearch nitric oxide transportsearch

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