1yen Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaP36A oxy (2MM IHP, 20% PEG) (10 test sets)

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 2.8 Å and deposited in 2004.

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 97%
C Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 97%
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 bicarbonate transportsearch hydrogen peroxide catabolic processsearch receptor-mediated endocytosissearch oxidation-reduction processsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch transportsearch positive regulation of cell deathsearch small molecule metabolic processsearch oxygen bindingsearch iron ion bindingsearch heme bindingsearch protein bindingsearch haptoglobin bindingsearch metal ion bindingsearch oxygen transporter activitysearch peroxidase activitysearch extracellular regionsearch blood microparticlesearch extracellular vesicular exosomesearch cytosolsearch hemoglobin complexsearch membranesearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch
B, D (P68871) response to hydrogen peroxidesearch renal absorptionsearch oxidation-reduction processsearch platelet aggregationsearch hydrogen peroxide catabolic processsearch regulation of blood pressuresearch protein heterooligomerizationsearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch receptor-mediated endocytosissearch small molecule metabolic processsearch blood coagulationsearch bicarbonate transportsearch positive regulation of cell deathsearch regulation of blood vessel sizesearch transportsearch nitric oxide transportsearch heme bindingsearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch protein bindingsearch oxygen transporter activitysearch oxygen bindingsearch hemoglobin bindingsearch iron ion bindingsearch cytosolsearch extracellular regionsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch blood microparticlesearch

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