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

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