1xye Summary

pdbe.org/1xye
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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) Cellular component (GO) Biological process (GO)
A, C (P69905) heme bindingsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch endocytic vesicle lumensearch blood microparticlesearch membranesearch cytosolsearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch oxygen transportsearch bicarbonate transportsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch transportsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch protein heterooligomerizationsearch oxidation-reduction processsearch
B, D (P68871) heme bindingsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch hemoglobin bindingsearch oxygen transporter activitysearch peroxidase activitysearch haptoglobin bindingsearch metal ion bindingsearch hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch cytosolsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch blood microparticlesearch oxygen transportsearch renal absorptionsearch blood coagulationsearch platelet aggregationsearch response to hydrogen peroxidesearch regulation of blood vessel sizesearch oxidation-reduction processsearch bicarbonate transportsearch nitric oxide transportsearch protein heterooligomerizationsearch transportsearch positive regulation of cell deathsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood pressuresearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch

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