1ydz Summary

pdbe.org/1ydz
spacer

T-To-T(High) quaternary transitions in human hemoglobin: alphaY140F oxy (2MM IHP, 20% PEG) (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 3.3 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 (2-140) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha chain P69905 (2-140) (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 - 140) 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 transportsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch bicarbonate transportsearch small molecule metabolic processsearch oxidation-reduction processsearch protein heterooligomerizationsearch receptor-mediated endocytosissearch response to hydrogen peroxidesearch hemoglobin complexsearch extracellular regionsearch cytosolsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch blood microparticlesearch membranesearch extracellular exosomesearch cytosolic small ribosomal subunitsearch iron ion bindingsearch oxygen bindingsearch heme bindingsearch haptoglobin bindingsearch protein bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch
B, D (P68871) oxygen transportsearch hydrogen peroxide catabolic processsearch nitric oxide transportsearch bicarbonate transportsearch oxidation-reduction processsearch receptor-mediated endocytosissearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch protein heterooligomerizationsearch small molecule metabolic processsearch renal absorptionsearch positive regulation of cell deathsearch platelet aggregationsearch regulation of blood pressuresearch transportsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch hemoglobin complexsearch cytosolsearch extracellular regionsearch extracellular exosomesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch endocytic vesicle lumensearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch hemoglobin bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch

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