1ye0 Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaV33A oxy (2MM IHP, 20% PEG) (1 test set)

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