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