1lfy Summary

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OXY HEMOGLOBIN (84% 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 3.3 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) transportsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch oxygen transportsearch bicarbonate transportsearch oxidation-reduction processsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch protein bindingsearch oxygen transporter activitysearch oxygen bindingsearch heme bindingsearch iron ion bindingsearch haptoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch membranesearch hemoglobin complexsearch endocytic vesicle lumensearch blood microparticlesearch cytosolsearch cytosolic small ribosomal subunitsearch
B (P68871) oxygen transportsearch blood coagulationsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch small molecule metabolic processsearch protein heterooligomerizationsearch renal absorptionsearch positive regulation of nitric oxide biosynthetic processsearch oxidation-reduction processsearch response to hydrogen peroxidesearch platelet aggregationsearch nitric oxide transportsearch regulation of blood vessel sizesearch regulation of blood pressuresearch transportsearch positive regulation of cell deathsearch protein bindingsearch heme bindingsearch iron ion bindingsearch oxygen bindingsearch hemoglobin bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch endocytic vesicle lumensearch cytosolsearch

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