1y7z Summary

pdbe.org/1y7z
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T-To-T(High) quaternary transitions in human hemoglobin: betaN108A deoxy low-salt (1 test set)

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