1ljw Summary

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Crystal Structure of Human Carbonmonoxy Hemoglobin at 2.16 A: A Snapshot of the Allosteric Transition

The structure was published by Safo, M.K., Burnett, J.C., Musayev, F.N., Nokuri, S., and Abraham, D.J., in 2002 in a paper entitled "Structure of human carbonmonoxyhemoglobin at 2.16 A: a snapshot of the allosteric transition." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.16 Å and deposited in 2002.

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%
B 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 (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

Chain InterPro annotation
A Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
B Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch