› 6cl4

X-ray diffraction
2.64Å resolution

LipC12 - Lipase from metagenomics

Released:
DOI: 10.2210/pdb6cl4/pdb
PDB entry 6cl4 coloured by chain, front view.
PDB entry 6cl4 coloured by chain, side view.
PDB entry 6cl4 coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Structure solution and analyses of the first true lipase obtained from metagenomics indicate potential for increased thermostability.
Martini VP, Krieger N, Glogauer A, Souza EM, Iulek J
N Biotechnol 53 65-72 (2019)
PMID: 31306784

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 33.43 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli
UniProt:
  • Canonical: G1APT8 (Residues: 1-293; Coverage: 100%)
Gene name: lipc12
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P4122
Unit cell:
a: 58.5Å b: 58.5Å c: 192.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.251
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Directed Evolution of Pseudomonas fluorescens Lipase Variants With Improved Thermostability Using Error-Prone PCR.
Guan et al. (2020)

2 mentions without citation

Mixed-valence tetranuclear manganese single-molecule magnets.
Yoo et al. (2001)
1 more