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

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