› 1r2g

X-ray diffraction
2.7Å resolution

Human Bcl-XL containing a Phe to Trp mutation at position 97

Released:
DOI: 10.2210/pdb1r2g/pdb
PDB entry 1r2g coloured by chain, front view.
PDB entry 1r2g coloured by chain, side view.
PDB entry 1r2g coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Bcl-XL mutations suppress cellular sensitivity to antimycin A.
Manion MK, O'Neill JW, Giedt CD, Kim KM, Zhang KY, Hockenbery DM
J Biol Chem 279 2159-65 (2004)
PMID: 14534311

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

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: 218 amino acids
Theoretical weight: 24.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07817 (Residues: 1-211; Coverage: 91%)
Gene names: BCL2L, BCL2L1, BCLX
Sequence domains:
Structure domains: Blc2-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P41212
Unit cell:
a: 64.39Å b: 64.39Å c: 110.984Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Mitochondrial membrane permeabilization in cell death.
Kroemer et al. (2007)
11 more

3 mentions without citation

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