1yen Summary

pdbe.org/1yen
spacer

T-To-T(High) quaternary transitions in human hemoglobin: betaP36A oxy (2MM IHP, 20% PEG) (10 test sets)

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 2.8 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 97%
C Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 97%
B Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) Hemoglobin alpha chain Homo sapiens
P68871 (2 - 147) 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 Cellular component (GO) Molecular function (GO) Biological process (GO)
A, C (P69905) hemoglobin complexsearch cytosolsearch extracellular regionsearch extracellular vesicular exosomesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch membranesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch oxygen bindingsearch heme bindingsearch protein bindingsearch iron ion bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch peroxidase activitysearch bicarbonate transportsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch oxygen transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch small molecule metabolic processsearch transportsearch positive regulation of cell deathsearch
B, D (P68871) cytosolsearch extracellular regionsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch hemoglobin complexsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch heme bindingsearch iron ion bindingsearch oxygen bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch metal ion bindingsearch oxygen transportsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch transportsearch renal absorptionsearch protein heterooligomerizationsearch regulation of blood vessel sizesearch small molecule metabolic processsearch positive regulation of nitric oxide biosynthetic processsearch blood coagulationsearch platelet aggregationsearch bicarbonate transportsearch regulation of blood pressuresearch positive regulation of cell deathsearch oxidation-reduction processsearch nitric oxide transportsearch

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