1thb Summary

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REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION

The structure was published by Waller, D.A. and Liddington, R.C., in 1990 in a paper entitled "Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 1990.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A (OXY) (ALPHA CHAIN) and HEMOGLOBIN A (DEOXY) (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 A (OXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN A (OXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN A (DEOXY) (BETA CHAIN) P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN A (DEOXY) (BETA CHAIN) P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) HEMOGLOBIN A (OXY) (ALPHA CHAIN) Homo sapiens
P68871 (2 - 147) HEMOGLOBIN A (DEOXY) (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 Biological process (GO) Cellular component (GO) Molecular function (GO)
A, C (P69905) oxygen transportsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch response to hydrogen peroxidesearch transportsearch receptor-mediated endocytosissearch protein heterooligomerizationsearch oxidation-reduction processsearch small molecule metabolic processsearch positive regulation of cell deathsearch hemoglobin complexsearch extracellular exosomesearch cytosolsearch endocytic vesicle lumensearch extracellular regionsearch cytosolic small ribosomal subunitsearch membranesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch
B, D (P68871) oxygen transportsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch positive regulation of nitric oxide biosynthetic processsearch small molecule metabolic processsearch response to hydrogen peroxidesearch regulation of blood pressuresearch renal absorptionsearch regulation of blood vessel sizesearch positive regulation of cell deathsearch oxidation-reduction processsearch transportsearch nitric oxide transportsearch protein heterooligomerizationsearch receptor-mediated endocytosissearch blood coagulationsearch platelet aggregationsearch hemoglobin complexsearch extracellular regionsearch blood microparticlesearch endocytic vesicle lumensearch cytosolsearch extracellular exosomesearch haptoglobin-hemoglobin complexsearch iron ion bindingsearch oxygen transporter activitysearch peroxidase activitysearch protein bindingsearch heme bindingsearch haptoglobin bindingsearch metal ion bindingsearch hemoglobin bindingsearch oxygen bindingsearch

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