1xzu Summary

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