› 2k89

Solution NMR

Solution structure of a novel Ubiquitin-binding domain from Human PLAA (PFUC, Gly76-Pro77 cis isomer)

Released:
DOI: 10.2210/pdb2k89/pdb
PDB entry 2k89 coloured by chain, ensemble of 15 models, front view.
PDB entry 2k89 coloured by chain, ensemble of 15 models, side view.
PDB entry 2k89 coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for ubiquitin recognition by a novel domain from human phospholipase A2-activating protein.
Fu QS, Zhou CJ, Gao HC, Jiang YJ, Zhou ZR, Hong J, Yao WM, Song AX, Lin DH, Hu HY
J Biol Chem 284 19043-52 (2009)
PMID: 19423704

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195104 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A-2-activating protein Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 9.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y263 (Residues: 386-465; Coverage: 10%)
Gene names: PLAA, PLAP
Sequence domains: PFU (PLAA family ubiquitin binding)
Structure domains: PFU (PLAA family ubiquitin binding), C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Ubiquitin and its binding domains.
Randles et al. (2012)
1 more

2 mentions without citation

Structural basis for ubiquitin recognition by a novel domain from human phospholipase A2-activating protein.
Fu et al. (2009)
1 more