1y8w Summary

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T-To-T(High) quaternary transitions in human hemoglobin: alphaR92A oxy (2mM IHP, 20% PEG) (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 2.9 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 Biological process (GO) Cellular component (GO) Molecular function (GO)
A, C (P69905) oxygen transportsearch response to hydrogen peroxidesearch bicarbonate transportsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch oxidation-reduction processsearch transportsearch positive regulation of cell deathsearch extracellular vesicular exosomesearch hemoglobin complexsearch extracellular regionsearch cytosolsearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch blood microparticlesearch haptoglobin-hemoglobin complexsearch membranesearch protein bindingsearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch peroxidase activitysearch metal ion bindingsearch
B, D (P68871) small molecule metabolic processsearch bicarbonate transportsearch regulation of blood pressuresearch hydrogen peroxide catabolic processsearch oxygen transportsearch protein heterooligomerizationsearch renal absorptionsearch nitric oxide transportsearch blood coagulationsearch positive regulation of cell deathsearch oxidation-reduction processsearch positive regulation of nitric oxide biosynthetic processsearch platelet aggregationsearch response to hydrogen peroxidesearch transportsearch regulation of blood vessel sizesearch extracellular regionsearch extracellular vesicular exosomesearch hemoglobin complexsearch blood microparticlesearch cytosolsearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch iron ion bindingsearch protein bindingsearch haptoglobin bindingsearch oxygen bindingsearch heme bindingsearch peroxidase activitysearch hemoglobin bindingsearch oxygen transporter activitysearch metal ion bindingsearch

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