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

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