1y4f Summary

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PDB entry 1y4f (supersedes 1a0w)

T-To-T(High) quaternary transitions in human hemoglobin: betaW37A deoxy low-salt (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 2.0 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 (2-147) (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 Molecular function (GO) Cellular component (GO) Biological process (GO)
A, C (P69905) iron ion bindingsearch heme bindingsearch metal ion bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch peroxidase activitysearch oxygen bindingsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch cytosolsearch extracellular vesicular exosomesearch extracellular regionsearch membranesearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch oxygen transportsearch bicarbonate transportsearch transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch response to hydrogen peroxidesearch small molecule metabolic processsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch
B, D (P68871) oxygen bindingsearch heme bindingsearch iron ion bindingsearch hemoglobin bindingsearch protein bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch haptoglobin bindingsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch cytosolsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch extracellular regionsearch blood microparticlesearch oxygen transportsearch oxidation-reduction processsearch renal absorptionsearch protein heterooligomerizationsearch bicarbonate transportsearch nitric oxide transportsearch regulation of blood pressuresearch transportsearch small molecule metabolic processsearch regulation of blood vessel sizesearch positive regulation of nitric oxide biosynthetic processsearch positive regulation of cell deathsearch blood coagulationsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic 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