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