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

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