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