› 4wmr

X-ray diffraction
1.7Å resolution

STRUCTURE OF MCL1 BOUND TO BRD inhibitor ligand 1 AT 1.7A

Released:
DOI: 10.2210/pdb4wmr/pdb
PDB entry 4wmr coloured by chain, front view.
PDB entry 4wmr coloured by chain, side view.
PDB entry 4wmr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1.
Clifton MC, Dranow DM, Leed A, Fulroth B, Fairman JW, Abendroth J, Atkins KA, Wallace E, Fan D, Xu G, Ni ZJ, Daniels D, Van Drie J, Wei G, Burgin AB, Golub TR, Hubbard BK, Serrano-Wu MH
PLoS One 10 e0125010 (2015)
PMID: 25909780

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-170534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Induced myeloid leukemia cell differentiation protein Mcl-1 Chain: A
Molecule details ›
Chain: A
Length: 150 amino acids
Theoretical weight: 17.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07820 (Residues: 173-321; Coverage: 43%)
Gene names: BCL2L3, MCL1
Sequence domains: Apoptosis regulator proteins, Bcl-2 family
Structure domains: Blc2-like

Ligands and Environments

3 bound ligands:
Ligand ZN 3 x ZN
Ligand 865 1 x 865
Ligand POP 2 x POP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 72.77Å b: 38.41Å c: 48.33Å
α: 90° β: 102.6° γ: 90°
R-values:
R R work R free
0.171 0.169 0.206
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Crystal structures of MBP fusion proteins.
Waugh DS. (2016)
1 more

3 mentions without citation

A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1.
Clifton et al. (2015)
2 more