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

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