1a3o Summary

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ARTIFICIAL MUTANT (ALPHA Y42H) OF DEOXY HEMOGLOBIN

The structure was published by Tame, J.R. and Vallone, B., in 2000 in a paper entitled "The structures of deoxy human haemoglobin and the mutant Hb Tyralpha42His at 120 K." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1998.

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%
C 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 99%
D HEMOGLOBIN (BETA CHAIN) P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 99%


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, C (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

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