1y35 Summary

pdbe.org/1y35
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T-To-T(High) quaternary transitions in human hemoglobin: betaY35F 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 2.12 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) protein bindingsearch peroxidase activitysearch oxygen bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch heme bindingsearch metal ion bindingsearch iron ion bindingsearch extracellular regionsearch cytosolic small ribosomal subunitsearch extracellular vesicular exosomesearch hemoglobin complexsearch blood microparticlesearch membranesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch cytosolsearch bicarbonate transportsearch protein heterooligomerizationsearch oxygen transportsearch response to hydrogen peroxidesearch transportsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch oxidation-reduction processsearch small molecule metabolic processsearch
B, D (P68871) heme bindingsearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch metal ion bindingsearch haptoglobin bindingsearch iron ion bindingsearch peroxidase activitysearch hemoglobin bindingsearch extracellular regionsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch extracellular vesicular exosomesearch endocytic vesicle lumensearch cytosolsearch oxygen transportsearch nitric oxide transportsearch response to hydrogen peroxidesearch blood coagulationsearch bicarbonate transportsearch oxidation-reduction processsearch regulation of blood vessel sizesearch transportsearch positive regulation of nitric oxide biosynthetic processsearch renal absorptionsearch positive regulation of cell deathsearch platelet aggregationsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch regulation of blood pressuresearch protein heterooligomerizationsearch

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