1ygf Summary

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T-to-T(high) quaternary transitions in human hemoglobin: betaH97A 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 2.7 Å and deposited in 2005.

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