1ye0 Summary

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

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