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

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