4q3o

X-ray diffraction
1.74Å resolution

Crystal structure of MGS-MT1, an alpha/beta hydrolase enzyme from a Lake Matapan deep-sea metagenome library

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-101010 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 348 amino acids
Theoretical weight: 38.44 KDa
Source organism: unidentified
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0B5KQQ5 (Residues: 1-348; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 189.454Å b: 131.397Å c: 112.441Å
α: 90° β: 103.55° γ: 90°
R-values:
R R work R free
0.147 0.145 0.185
Expression system: Escherichia coli BL21(DE3)