› 2av9

X-ray diffraction
2.4Å resolution

Crystal Structure of the PA5185 protein from Pseudomonas Aeruginosa Strain PAO1.

Released:
DOI: 10.2210/pdb2av9/pdb
PDB entry 2av9 coloured by chain, front view.
PDB entry 2av9 coloured by chain, side view.
PDB entry 2av9 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Function-biased choice of additives for optimization of protein crystallization - the case of the putative thioesterase PA5185 from Pseudomonas aeruginosa PAO1.
Chruszcz M, Zimmerman MD, Wang S, Koclega KD, Zheng H, Evdokimova E, Kudritska M, Cymborowski M, Savchenko A, Edwards A, Minor W
Cryst Growth Des 8 4054-4061 (2008)
PMID: 19898606

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioesterase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 147 amino acids
Theoretical weight: 16.53 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HU04 (Residues: 1-147; Coverage: 100%)
Gene name: PA5185
Sequence domains: Thioesterase superfamily
Structure domains: Hotdog Thioesterase

Ligands and Environments

1 bound ligand:
Ligand SO4 15 x SO4
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 241.661Å b: 64.384Å c: 117.469Å
α: 90° β: 105.4° γ: 90°
R-values:
R R work R free
0.207 0.204 0.253
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Benefits of structural genomics for drug discovery research.
Grabowski et al. (2009)
2 other articles

3 mentions without citation

Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins.
Pidugu et al. (2009)
2 more