1yih Summary

pdbe.org/1yih
spacer

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