1ygd Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaW37E alpha zinc beta oxy (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 2.73 Å and deposited in 2005.

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