1yg5 Summary

pdbe.org/1yg5
spacer

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 Molecular function (GO) Biological process (GO) Cellular component (GO)
A, C (P69905) heme bindingsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch oxygen transportsearch protein heterooligomerizationsearch bicarbonate transportsearch small molecule metabolic processsearch response to hydrogen peroxidesearch oxidation-reduction processsearch hydrogen peroxide catabolic processsearch transportsearch positive regulation of cell deathsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch extracellular regionsearch cytosolsearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch cytosolic small ribosomal subunitsearch blood microparticlesearch membranesearch
B, D (P68871) iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch hemoglobin bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transporter activitysearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood pressuresearch platelet aggregationsearch protein heterooligomerizationsearch bicarbonate transportsearch renal absorptionsearch nitric oxide transportsearch regulation of blood vessel sizesearch transportsearch positive regulation of cell deathsearch small molecule metabolic processsearch blood coagulationsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch response to hydrogen peroxidesearch hemoglobin complexsearch blood microparticlesearch extracellular regionsearch cytosolsearch extracellular vesicular exosomesearch 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