1lfv Summary

pdbe.org/1lfv
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OXY HEMOGLOBIN (88% 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 2.8 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) Cellular component (GO) Biological process (GO)
A (P69905) oxygen bindingsearch iron ion bindingsearch heme bindingsearch protein bindingsearch oxygen transporter activitysearch peroxidase activitysearch metal ion bindingsearch haptoglobin bindingsearch hemoglobin complexsearch cytosolic small ribosomal subunitsearch extracellular regionsearch cytosolsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch membranesearch blood microparticlesearch endocytic vesicle lumensearch oxygen transportsearch bicarbonate transportsearch receptor-mediated endocytosissearch transportsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch small molecule metabolic processsearch oxidation-reduction processsearch
B (P68871) iron ion bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transporter activitysearch heme bindingsearch haptoglobin bindingsearch hemoglobin bindingsearch hemoglobin complexsearch extracellular regionsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch cytosolsearch blood microparticlesearch extracellular vesicular exosomesearch regulation of blood vessel sizesearch oxidation-reduction processsearch transportsearch bicarbonate transportsearch oxygen transportsearch regulation of blood pressuresearch positive regulation of nitric oxide biosynthetic processsearch response to hydrogen peroxidesearch small molecule metabolic processsearch positive regulation of cell deathsearch nitric oxide transportsearch hydrogen peroxide catabolic processsearch receptor-mediated endocytosissearch renal absorptionsearch blood coagulationsearch protein heterooligomerizationsearch platelet aggregationsearch

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