1a3n Summary

pdbe.org/1a3n
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DEOXY HUMAN 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 oxygen bindingsearch heme bindingsearch protein bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch oxygen transportsearch small molecule metabolic processsearch oxidation-reduction processsearch bicarbonate transportsearch receptor-mediated endocytosissearch transportsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch hemoglobin complexsearch cytosolic small ribosomal subunitsearch cytosolsearch extracellular regionsearch extracellular exosomesearch membranesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch endocytic vesicle lumensearch
B, D (P68871) heme bindingsearch iron ion bindingsearch protein bindingsearch oxygen bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch oxygen transportsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch nitric oxide transportsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood vessel sizesearch oxidation-reduction processsearch receptor-mediated endocytosissearch regulation of blood pressuresearch blood coagulationsearch bicarbonate transportsearch platelet aggregationsearch renal absorptionsearch protein heterooligomerizationsearch small molecule metabolic processsearch response to hydrogen peroxidesearch transportsearch extracellular regionsearch endocytic vesicle lumensearch extracellular exosomesearch cytosolsearch blood microparticlesearch hemoglobin complexsearch 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