1sdk 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) Cellular component (GO) Biological process (GO)
A, C (P69905) heme bindingsearch iron ion bindingsearch oxygen transporter activitysearch protein bindingsearch peroxidase activitysearch oxygen bindingsearch metal ion bindingsearch haptoglobin bindingsearch extracellular regionsearch blood microparticlesearch hemoglobin complexsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch cytosolsearch membranesearch haptoglobin-hemoglobin complexsearch bicarbonate transportsearch transportsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch oxidation-reduction processsearch oxygen transportsearch small molecule metabolic processsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch
B, D (P68871) heme bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch hemoglobin bindingsearch metal ion bindingsearch oxygen bindingsearch oxygen transporter activitysearch iron ion bindingsearch haptoglobin-hemoglobin complexsearch extracellular regionsearch hemoglobin complexsearch cytosolsearch blood microparticlesearch endocytic vesicle lumensearch extracellular vesicular exosomesearch positive regulation of cell deathsearch blood coagulationsearch small molecule metabolic processsearch renal absorptionsearch hydrogen peroxide catabolic processsearch oxygen transportsearch nitric oxide transportsearch platelet aggregationsearch response to hydrogen peroxidesearch regulation of blood pressuresearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood vessel sizesearch bicarbonate transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch transportsearch

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