1xye Summary

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T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt

The structure was published by Kavanaugh, J.S., Rogers, P.H., Arnone, A., et al., Juszczak, L.J., Peterson, E.S., and Friedman, J.M., in 2005 in a paper entitled "Intersubunit interactions associated with tyr42alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.13 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 (3-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha chain P69905 (3-142) (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 (3 - 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) Biological process (GO) Cellular component (GO)
A, C (P69905) heme bindingsearch iron ion bindingsearch oxygen transporter activitysearch protein bindingsearch haptoglobin bindingsearch oxygen bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transportsearch bicarbonate transportsearch transportsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch protein heterooligomerizationsearch oxidation-reduction processsearch hemoglobin complexsearch membranesearch extracellular regionsearch endocytic vesicle lumensearch blood microparticlesearch cytosolsearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch
B, D (P68871) oxygen transporter activitysearch hemoglobin bindingsearch protein bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen bindingsearch haptoglobin bindingsearch iron ion bindingsearch heme bindingsearch bicarbonate transportsearch nitric oxide transportsearch blood coagulationsearch oxygen transportsearch response to hydrogen peroxidesearch transportsearch platelet aggregationsearch renal absorptionsearch protein heterooligomerizationsearch regulation of blood vessel sizesearch positive regulation of cell deathsearch positive regulation of nitric oxide biosynthetic processsearch oxidation-reduction processsearch regulation of blood pressuresearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch extracellular regionsearch endocytic vesicle lumensearch hemoglobin complexsearch extracellular vesicular exosomesearch cytosolsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch

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