1yih Summary

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T-to-T(High) quaternary transitions in human hemoglobin: betaP100A oxy (2.2MM 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 2.0 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 Not available
Homo sapienssearch 99% 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) Molecular function (GO) Cellular component (GO)
A, C (P69905) transportsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch oxygen transportsearch bicarbonate transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch haptoglobin bindingsearch heme bindingsearch iron ion bindingsearch protein bindingsearch metal ion bindingsearch oxygen transporter activitysearch peroxidase activitysearch oxygen bindingsearch hemoglobin complexsearch extracellular regionsearch cytosolic small ribosomal subunitsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch cytosolsearch membranesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch
B, D (P68871) response to hydrogen peroxidesearch bicarbonate transportsearch nitric oxide transportsearch renal absorptionsearch positive regulation of cell deathsearch regulation of blood vessel sizesearch regulation of blood pressuresearch platelet aggregationsearch oxygen transportsearch transportsearch blood coagulationsearch oxidation-reduction processsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch positive regulation of nitric oxide biosynthetic processsearch oxygen bindingsearch heme bindingsearch metal ion bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch peroxidase activitysearch hemoglobin bindingsearch iron ion bindingsearch cytosolsearch extracellular regionsearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch endocytic vesicle lumensearch

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