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