1y4g Summary

pdbe.org/1y4g
spacer

PDB entry 1y4g (supersedes 1a0x)

T-To-T(High) quaternary transitions in human hemoglobin: betaW37G 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 1.91 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 protein bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch peroxidase activitysearch hemoglobin complexsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch cytosolsearch extracellular regionsearch membranesearch blood microparticlesearch cytosolic small ribosomal subunitsearch oxygen transportsearch bicarbonate transportsearch oxidation-reduction processsearch small molecule metabolic processsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch transportsearch positive regulation of cell deathsearch
B, D (P68871) oxygen bindingsearch heme bindingsearch iron ion bindingsearch haptoglobin bindingsearch protein bindingsearch oxygen transporter activitysearch metal ion bindingsearch hemoglobin bindingsearch peroxidase activitysearch hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch extracellular regionsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch oxygen transportsearch response to hydrogen peroxidesearch transportsearch positive regulation of cell deathsearch protein heterooligomerizationsearch small molecule metabolic processsearch regulation of blood pressuresearch blood coagulationsearch oxidation-reduction processsearch nitric oxide transportsearch regulation of blood vessel sizesearch bicarbonate transportsearch renal absorptionsearch hydrogen peroxide catabolic processsearch platelet aggregationsearch positive regulation of nitric oxide biosynthetic 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