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

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