1cls Summary

pdbe.org/1cls
spacer

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

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