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