1lfq Summary

pdbe.org/1lfq
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OXY HEMOGLOBIN (93% 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 Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P69905) heme bindingsearch oxygen bindingsearch iron ion bindingsearch protein bindingsearch peroxidase activitysearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch oxygen transportsearch hydrogen peroxide catabolic processsearch receptor-mediated endocytosissearch oxidation-reduction processsearch protein heterooligomerizationsearch positive regulation of cell deathsearch bicarbonate transportsearch small molecule metabolic processsearch transportsearch response to hydrogen peroxidesearch extracellular exosomesearch extracellular regionsearch endocytic vesicle lumensearch hemoglobin complexsearch cytosolsearch membranesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch cytosolic small ribosomal subunitsearch
B (P68871) oxygen bindingsearch iron ion bindingsearch oxygen transporter activitysearch protein bindingsearch haptoglobin bindingsearch metal ion bindingsearch hemoglobin bindingsearch peroxidase activitysearch heme bindingsearch oxygen transportsearch bicarbonate transportsearch renal absorptionsearch positive regulation of nitric oxide biosynthetic processsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch receptor-mediated endocytosissearch nitric oxide transportsearch regulation of blood pressuresearch blood coagulationsearch platelet aggregationsearch transportsearch response to hydrogen peroxidesearch oxidation-reduction processsearch regulation of blood vessel sizesearch protein heterooligomerizationsearch positive regulation of cell deathsearch hemoglobin complexsearch extracellular regionsearch cytosolsearch extracellular exosomesearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch 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