1ydz Summary

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