1y4p Summary

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

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