1xxt Summary

pdbe.org/1xxt
spacer

The T-to-T High Transitions in Human Hemoglobin: wild-type deoxy Hb A (low salt, one test set)

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

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