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