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

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