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

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