1y85 Summary

pdbe.org/1y85
spacer

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