1cls Summary

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CROSS-LINKED HUMAN HEMOGLOBIN DEOXY

The structure was published by Bucci, E., Razynska, A., Kwansa, H., et al., Moult, J., Ji, X., and Gilliland, G., in 1996 in a paper entitled "Positive and negative cooperativities at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1995.

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

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

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

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