1yg5 Summary

pdbe.org/1yg5
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T-To-T(High) quaternary transitions in human hemoglobin: betaW37H 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 2.7 Å and deposited in 2005.

The experimental data on which the structure is based was not 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 Biological process (GO) Molecular function (GO) Cellular component (GO)
A, C (P69905) oxygen transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch receptor-mediated endocytosissearch bicarbonate transportsearch small molecule metabolic processsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch transportsearch positive regulation of cell deathsearch oxygen bindingsearch iron ion bindingsearch heme bindingsearch haptoglobin bindingsearch protein bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch endocytic vesicle lumensearch extracellular regionsearch cytosolsearch extracellular exosomesearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch blood microparticlesearch membranesearch
B, D (P68871) oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood vessel sizesearch oxidation-reduction processsearch protein heterooligomerizationsearch platelet aggregationsearch bicarbonate transportsearch nitric oxide transportsearch blood coagulationsearch renal absorptionsearch regulation of blood pressuresearch positive regulation of cell deathsearch response to hydrogen peroxidesearch small molecule metabolic processsearch transportsearch hydrogen peroxide catabolic processsearch receptor-mediated endocytosissearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch haptoglobin bindingsearch protein bindingsearch hemoglobin bindingsearch oxygen transporter activitysearch peroxidase activitysearch metal ion bindingsearch hemoglobin complexsearch blood microparticlesearch cytosolsearch extracellular exosomesearch extracellular regionsearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch

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