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

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