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