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