1lft Summary

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OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)

The structure was published by Biswal, B.K. and Vijayan, M., in 2002 in a paper entitled "Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: variability in the T state." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 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 bicarbonate transportsearch transportsearch positive regulation of cell deathsearch receptor-mediated endocytosissearch small molecule metabolic processsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch oxidation-reduction processsearch heme bindingsearch oxygen bindingsearch iron ion bindingsearch protein bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch haptoglobin bindingsearch hemoglobin complexsearch membranesearch extracellular regionsearch haptoglobin-hemoglobin complexsearch cytosolsearch extracellular exosomesearch blood microparticlesearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch
B (P68871) oxygen transportsearch bicarbonate transportsearch protein heterooligomerizationsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch regulation of blood vessel sizesearch oxidation-reduction processsearch renal absorptionsearch hydrogen peroxide catabolic processsearch regulation of blood pressuresearch positive regulation of nitric oxide biosynthetic processsearch nitric oxide transportsearch small molecule metabolic processsearch transportsearch blood coagulationsearch receptor-mediated endocytosissearch platelet aggregationsearch heme bindingsearch iron ion bindingsearch protein bindingsearch hemoglobin bindingsearch metal ion bindingsearch oxygen bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch peroxidase activitysearch hemoglobin complexsearch extracellular exosomesearch haptoglobin-hemoglobin complexsearch cytosolsearch extracellular regionsearch blood microparticlesearch endocytic vesicle lumensearch

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