› 2o2m

Solution NMR

Solution structure of the anti-apoptotic protein Bcl-xL in complex with an acyl-sulfonamide-based ligand

Released:
DOI: 10.2210/pdb2o2m/pdb
PDB entry 2o2m coloured by chain, front view.
PDB entry 2o2m coloured by chain, side view.
PDB entry 2o2m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Studies leading to potent, dual inhibitors of Bcl-2 and Bcl-xL.
Bruncko M, Oost TK, Belli BA, Ding H, Joseph MK, Kunzer A, Martineau D, McClellan WJ, Mitten M, Ng SC, Nimmer PM, Oltersdorf T, Park CM, Petros AM, Shoemaker AR, Song X, Wang X, Wendt MD, Zhang H, Fesik SW, Rosenberg SH, Elmore SW
J Med Chem 50 641-62 (2007)
PMID: 17256834

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bcl-2-like protein 1 Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 16.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07817 (Residues: 2-20, 22-23, 52-196; Coverage: 59%)
Gene names: BCL2L, BCL2L1, BCLX
Sequence domains:
Structure domains: Blc2-like

Ligands and Environments

1 bound ligand:
Ligand LI0 1 x LI0
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

35 review citations

Reaching for high-hanging fruit in drug discovery at protein-protein interfaces.
Wells et al. (2007)
34 more

5 mentions without citation

The Structural Biology of Bcl-xL.
Lee et al. (2019)
4 more