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

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