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