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