1xzv Summary

pdbe.org/1xzv
spacer

T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaP95A 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 2.11 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) iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch metal ion bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transportsearch small molecule metabolic processsearch protein heterooligomerizationsearch positive regulation of cell deathsearch oxidation-reduction processsearch bicarbonate transportsearch response to hydrogen peroxidesearch transportsearch hydrogen peroxide catabolic processsearch extracellular regionsearch cytosolsearch extracellular vesicular exosomesearch hemoglobin complexsearch endocytic vesicle lumensearch blood microparticlesearch membranesearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch
B, D (P68871) iron ion bindingsearch heme bindingsearch protein bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch oxygen bindingsearch hemoglobin bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transportsearch oxidation-reduction processsearch bicarbonate transportsearch renal absorptionsearch small molecule metabolic processsearch protein heterooligomerizationsearch nitric oxide transportsearch blood coagulationsearch regulation of blood pressuresearch regulation of blood vessel sizesearch hydrogen peroxide catabolic processsearch platelet aggregationsearch positive regulation of nitric oxide biosynthetic processsearch transportsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch cytosolsearch blood microparticlesearch endocytic vesicle lumensearch

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