1xz2 Summary

pdbe.org/1xz2
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wild-type hemoglobin deoxy no-salt

The structure was published by Kavanaugh, J.S., Rogers, P.H., Arnone, A., et al., Juszczak, L.J., Peterson, E.S., and Friedman, J.M., in 2005 in a paper entitled "Intersubunit interactions associated with tyr42alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 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) Cellular component (GO) Molecular function (GO)
A, C (P69905) oxygen transportsearch small molecule metabolic processsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch positive regulation of cell deathsearch transportsearch oxidation-reduction processsearch protein heterooligomerizationsearch extracellular vesicular exosomesearch hemoglobin complexsearch extracellular regionsearch cytosolsearch membranesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch blood microparticlesearch haptoglobin-hemoglobin complexsearch protein bindingsearch heme bindingsearch oxygen bindingsearch iron ion bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch haptoglobin bindingsearch
B, D (P68871) oxygen transportsearch nitric oxide transportsearch regulation of blood pressuresearch bicarbonate transportsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch transportsearch platelet aggregationsearch positive regulation of nitric oxide biosynthetic processsearch positive regulation of cell deathsearch blood coagulationsearch regulation of blood vessel sizesearch oxidation-reduction processsearch renal absorptionsearch blood microparticlesearch extracellular regionsearch endocytic vesicle lumensearch cytosolsearch hemoglobin complexsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch oxygen bindingsearch peroxidase activitysearch protein bindingsearch oxygen transporter activitysearch heme bindingsearch iron ion bindingsearch hemoglobin bindingsearch haptoglobin bindingsearch metal ion bindingsearch

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