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

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