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

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