1lfz Summary

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OXY HEMOGLOBIN (25% METHANOL)

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

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