› 4oq5

X-ray diffraction
2.86Å resolution

Crystal Structure of Human MCL-1 Bound to Inhibitor 4-(4-methylnaphthalen-1-yl)-2-{[(4-phenoxyphenyl)sulfonyl]amino}benzoic acid

Released:
DOI: 10.2210/pdb4oq5/pdb
PDB entry 4oq5 coloured by chain, front view.
PDB entry 4oq5 coloured by chain, side view.
PDB entry 4oq5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Fragment-based discovery of potent inhibitors of the anti-apoptotic MCL-1 protein.
Petros AM, Swann SL, Song D, Swinger K, Park C, Zhang H, Wendt MD, Kunzer AR, Souers AJ, Sun C
Bioorg Med Chem Lett 24 1484-8 (2014)
PMID: 24582986

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-170534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Induced myeloid leukemia cell differentiation protein Mcl-1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 163 amino acids
Theoretical weight: 18.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07820 (Residues: 174-326; Coverage: 44%)
Gene names: BCL2L3, MCL1
Sequence domains: Apoptosis regulator proteins, Bcl-2 family
Structure domains: Blc2-like

Ligands and Environments

1 bound ligand:
Ligand 2UU 6 x 2UU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 71.112Å b: 109.75Å c: 76.544Å
α: 90° β: 93.31° γ: 90°
R-values:
R R work R free
0.2 0.198 0.239
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Twenty years on: the impact of fragments on drug discovery.
Erlanson et al. (2016)
11 more

6 mentions without citation

Small molecule Mcl-1 inhibitors for the treatment of cancer.
Belmar et al. (2015)
5 more