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

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