1xzu Summary

pdbe.org/1xzu
spacer

T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaD94G deoxy low-salt

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