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