› 6emr

Solution NMR

Solution structure of the LEDGF/p75 IBD - IWS1 (aa 446-548) complex

Released:
DOI: 10.2210/pdb6emr/pdb
PDB entry 6emr coloured by chain, ensemble of 40 models, front view.
PDB entry 6emr coloured by chain, ensemble of 40 models, side view.
PDB entry 6emr coloured by chain, ensemble of 40 models, top view.
Source organism: Homo sapiens
Primary publication:
Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation.
Sharma S, Čermáková K, De Rijck J, Demeulemeester J, Fábry M, El Ashkar S, Van Belle S, Lepšík M, Tesina P, Duchoslav V, Novák P, Hubálek M, Srb P, Christ F, Řezáčová P, Hodges HC, Debyser Z, Veverka V
Proc Natl Acad Sci U S A 115 E7053-E7062 (2018)
PMID: 29997176

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130984 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PC4 and SFRS1-interacting protein; Protein IWS1 homolog Chain: A
Molecule details ›
Chain: A
Length: 206 amino acids
Theoretical weight: 23.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75475 (Residues: 345-442; Coverage: 19%)
  • Canonical: Q96ST2 (Residues: 447-548; Coverage: 13%)
Gene names: DFS70, IWS1, IWS1L, LEDGF, PSIP1, PSIP2
Sequence domains: Lens epithelium-derived growth factor (LEDGF)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Anti-DFS70 antibodies: an update on our current understanding and their clinical usefulness.
Mahler et al. (2019)
7 more

1 mention without citation

Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation.
Sharma et al. (2018)