2nl9

X-ray diffraction
1.55Å resolution

Crystal structure of the Mcl-1:Bim BH3 complex

Released:
Source organisms:
Primary publication:
Structural insights into the degradation of Mcl-1 induced by BH3 domains.
Proc. Natl. Acad. Sci. U.S.A. 104 6217-22 (2007)
PMID: 17389404

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
Non-polymer only dimer (preferred)
Non-polymer only octamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Induced myeloid leukemia cell differentiation protein Mcl-1; Induced myeloid leukemia cell differentiation protein Mcl-1 homolog Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.91 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07820 (Residues: 241-327; Coverage: 25%)
  • Canonical: P97287 (Residues: 152-221; Coverage: 21%)
Gene names: BCL2L3, MCL1, Mcl1
Structure domains: Blc2-like
Bcl-2-like protein 11 Chain: B
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 3.27 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: O43521 (Residues: 141-166; Coverage: 13%)
Gene names: BCL2L11, BIM

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: I222
Unit cell:
a: 52.38Å b: 70.08Å c: 117.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.203
Expression system: Escherichia coli BL21(DE3)