1y85 Summary

pdbe.org/1y85
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PDB entry 1y85 (supersedes 1axf)

T-To-T(High) quaternary transitions in human hemoglobin: desHIS146beta deoxy low-salt

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 2.13 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 (2-146) (HBB_HUMAN)search Homo sapienssearch 98% 145 100%
D Hemoglobin beta chain P68871 (2-146) (HBB_HUMAN)search Homo sapienssearch 98% 145 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) Hemoglobin alpha chain Homo sapiens
P68871 (2 - 146) 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 hydrogen peroxide catabolic processsearch oxidation-reduction processsearch bicarbonate transportsearch small molecule metabolic processsearch transportsearch positive regulation of cell deathsearch protein heterooligomerizationsearch heme bindingsearch iron ion bindingsearch oxygen bindingsearch oxygen transporter activitysearch protein bindingsearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch cytosolic small ribosomal subunitsearch extracellular regionsearch extracellular vesicular exosomesearch blood microparticlesearch cytosolsearch membranesearch endocytic vesicle lumensearch
B, D (P68871) oxygen transportsearch transportsearch nitric oxide transportsearch regulation of blood pressuresearch bicarbonate transportsearch positive regulation of cell deathsearch renal absorptionsearch response to hydrogen peroxidesearch small molecule metabolic processsearch blood coagulationsearch regulation of blood vessel sizesearch oxidation-reduction processsearch platelet aggregationsearch positive regulation of nitric oxide biosynthetic processsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch oxygen bindingsearch iron ion bindingsearch heme bindingsearch protein bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch peroxidase activitysearch metal ion bindingsearch haptoglobin bindingsearch extracellular regionsearch hemoglobin complexsearch cytosolsearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch blood microparticlesearch extracellular vesicular exosomesearch

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