1yeq Summary

pdbe.org/1yeq
spacer

T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y OXY (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 2.75 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% 141 100%
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 blood microparticlesearch cytosolsearch extracellular regionsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch membranesearch protein bindingsearch oxygen transporter activitysearch heme bindingsearch metal ion bindingsearch oxygen bindingsearch haptoglobin bindingsearch peroxidase activitysearch iron ion bindingsearch oxygen transportsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch protein heterooligomerizationsearch small molecule metabolic processsearch oxidation-reduction processsearch transportsearch response to hydrogen peroxidesearch
B, D (P68871) hemoglobin complexsearch cytosolsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch extracellular vesicular exosomesearch extracellular regionsearch endocytic vesicle lumensearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch metal ion bindingsearch haptoglobin bindingsearch heme bindingsearch hemoglobin bindingsearch peroxidase activitysearch iron ion bindingsearch protein heterooligomerizationsearch nitric oxide transportsearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch blood coagulationsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch renal absorptionsearch regulation of blood vessel sizesearch oxidation-reduction processsearch regulation of blood pressuresearch small molecule metabolic processsearch response to hydrogen peroxidesearch platelet aggregationsearch bicarbonate transportsearch transportsearch

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