› 4txr

X-ray diffraction
1Å resolution

Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM and CHMP5 MIM

Released:
DOI: 10.2210/pdb4txr/pdb
PDB entry 4txr coloured by chain, front view.
PDB entry 4txr coloured by chain, side view.
PDB entry 4txr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A novel mechanism of regulating the ATPase VPS4 by its cofactor LIP5 and the endosomal sorting complex required for transport (ESCRT)-III protein CHMP5.
Vild CJ, Li Y, Guo EZ, Liu Y, Xu Z
J Biol Chem 290 7291-303 (2015)
PMID: 25637630

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-181643 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Charged multivesicular body protein 1b Chain: B
Molecule details ›
Chain: B
Length: 25 amino acids
Theoretical weight: 2.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7LBR1 (Residues: 176-199; Coverage: 12%)
Gene names: C18orf2, CHMP1B
Vacuolar protein sorting-associated protein VTA1 homolog Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NP79 (Residues: 1-162; Coverage: 53%)
Gene names: C6orf55, HSPC228, My012, VTA1
Sequence domains: Vta1 like
Structure domains: Vacuolar protein sorting-associated protein vta1
Charged multivesicular body protein 5 Chain: C
Molecule details ›
Chain: C
Length: 58 amino acids
Theoretical weight: 6.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NZZ3 (Residues: 139-195; Coverage: 26%)
Gene names: C9orf83, CGI-34, CHMP5, HSPC177, PNAS-114, PNAS-2, SNF7DC2
Sequence domains: Snf7

Ligands and Environments

2 bound ligands:
Ligand ACT 1 x ACT
Ligand EDO 9 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 34.197Å b: 60.567Å c: 52.048Å
α: 90° β: 90.39° γ: 90°
R-values:
R R work R free
0.164 0.164 0.18
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.
Monroe et al. (2016)
3 more

3 mentions without citation

Insights into Thiol-Aromatic Interactions: A Stereoelectronic Basis for S-H/π Interactions.
Forbes et al. (2017)
2 more