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

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