1sdl Summary

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CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A

The structure was published by Schumacher, M.A., Dixon, M.M., Kluger, R., Jones, R.T., and Brennan, R.G., in 1995 in a paper entitled "Allosteric transition intermediates modelled by crosslinked haemoglobins." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1996.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN A P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN A P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN A 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 Homo sapiens
P68871 (2 - 147) HEMOGLOBIN A 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) oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch heme bindingsearch peroxidase activitysearch iron ion bindingsearch oxygen transporter activitysearch metal ion bindingsearch oxygen transportsearch bicarbonate transportsearch protein heterooligomerizationsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch oxidation-reduction processsearch transportsearch response to hydrogen peroxidesearch cytosolsearch extracellular regionsearch membranesearch extracellular vesicular exosomesearch hemoglobin complexsearch blood microparticlesearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch
B, D (P68871) oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch heme bindingsearch peroxidase activitysearch haptoglobin bindingsearch hemoglobin bindingsearch metal ion bindingsearch iron ion bindingsearch oxygen transportsearch response to hydrogen peroxidesearch blood coagulationsearch positive regulation of cell deathsearch regulation of blood vessel sizesearch oxidation-reduction processsearch bicarbonate transportsearch nitric oxide transportsearch protein heterooligomerizationsearch small molecule metabolic processsearch regulation of blood pressuresearch hydrogen peroxide catabolic processsearch transportsearch positive regulation of nitric oxide biosynthetic processsearch renal absorptionsearch platelet aggregationsearch extracellular regionsearch hemoglobin complexsearch blood microparticlesearch cytosolsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch

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