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