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

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