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

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