1y46 Summary

pdbe.org/1y46
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PDB entry 1y46 (supersedes 1a0v)

T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y deoxy low-salt (10 test sets)

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

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