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

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