1y4p Summary

pdbe.org/1y4p
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PDB entry 1y4p (supersedes 1a0y)

T-To-T(high) quaternary transitions in human hemoglobin: betaW37E 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 1.98 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) heme bindingsearch iron ion bindingsearch oxygen bindingsearch peroxidase activitysearch oxygen transporter activitysearch protein bindingsearch haptoglobin bindingsearch metal ion bindingsearch hemoglobin complexsearch endocytic vesicle lumensearch extracellular regionsearch blood microparticlesearch extracellular vesicular exosomesearch membranesearch cytosolsearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch oxygen transportsearch response to hydrogen peroxidesearch transportsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch bicarbonate transportsearch positive regulation of cell deathsearch oxidation-reduction processsearch protein heterooligomerizationsearch
B, D (P68871) heme bindingsearch iron ion bindingsearch haptoglobin bindingsearch protein bindingsearch peroxidase activitysearch oxygen transporter activitysearch oxygen bindingsearch hemoglobin bindingsearch metal ion bindingsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch extracellular regionsearch cytosolsearch blood microparticlesearch oxygen transportsearch bicarbonate transportsearch response to hydrogen peroxidesearch regulation of blood vessel sizesearch renal absorptionsearch positive regulation of nitric oxide biosynthetic processsearch small molecule metabolic processsearch platelet aggregationsearch positive regulation of cell deathsearch nitric oxide transportsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch transportsearch blood coagulationsearch regulation of blood pressuresearch

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