1k1k Summary

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Structure of Mutant Human Carbonmonoxyhemoglobin C (beta E6K) at 2.0 Angstrom Resolution in Phosphate Buffer.

The structure was published by Dewan, J.C., Feeling-Taylor, A., Puius, Y.A., et al., Nagel, R.L., Almo, S.C., and Hirsch, R.E., in 2002 in a paper entitled "Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2001.

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%
B HEMOGLOBIN 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 ALPHA CHAIN Homo sapiens
P68871 (2 - 147) HEMOGLOBIN BETA CHAIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

Chain InterPro annotation
A Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
B Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch