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

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