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