1xy0 Summary

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T-to-THigh Transitions in Human Hemoglobin: alphaK40G deoxy low-salt

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