1yie Summary

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T-to-thigh quaternary transitions in human hemoglobin: betaW37A oxy (2.2MM IHP, 13% 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 2.4 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) oxygen bindingsearch iron ion bindingsearch protein bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch heme bindingsearch hemoglobin complexsearch membranesearch extracellular regionsearch extracellular vesicular exosomesearch blood microparticlesearch cytosolsearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch small molecule metabolic processsearch oxidation-reduction processsearch oxygen transportsearch protein heterooligomerizationsearch positive regulation of cell deathsearch transportsearch
B, D (P68871) oxygen transporter activitysearch protein bindingsearch oxygen bindingsearch iron ion bindingsearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch hemoglobin bindingsearch heme bindingsearch extracellular regionsearch hemoglobin complexsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch blood microparticlesearch haptoglobin-hemoglobin complexsearch cytosolsearch oxygen transportsearch renal absorptionsearch platelet aggregationsearch transportsearch small molecule metabolic processsearch bicarbonate transportsearch blood coagulationsearch hydrogen peroxide catabolic processsearch regulation of blood pressuresearch regulation of blood vessel sizesearch positive regulation of cell deathsearch protein heterooligomerizationsearch oxidation-reduction processsearch positive regulation of nitric oxide biosynthetic processsearch nitric oxide transportsearch response to hydrogen peroxidesearch

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