› 7vpb

X-ray diffraction
1.68Å resolution

Crystal structure of a novel hydrolase in apo form

Released:
DOI: 10.2210/pdb7vpb/pdb
PDB entry 7vpb coloured by chain, front view.
PDB entry 7vpb coloured by chain, side view.
PDB entry 7vpb coloured by chain, top view.
Source organism: unclassified Marinobacter
Primary publication:
Structural insight and engineering of a plastic degrading hydrolase Ple629.
Li Z, Zhao Y, Wu P, Wang H, Li Q, Gao J, Qin HM, Wei H, Bornscheuer UT, Han X, Wei R, Liu W
Biochem Biophys Res Commun 626 100-106 (2022)
PMID: 35981419

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
plastic degrading hydrolase Ple629 Chains: A, B
Molecule details ›
Chains: A, B
Length: 291 amino acids
Theoretical weight: 30.29 KDa
Source organism: unclassified Marinobacter
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

2 bound ligands:
Ligand ACT 2 x ACT
Ligand J1K 1 x J1K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P32
Unit cell:
a: 71.607Å b: 71.607Å c: 87.327Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.155 0.177
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Trends in in-silico guided engineering of efficient polyethylene terephthalate (PET) hydrolyzing enzymes to enable bio-recycling and upcycling of PET.
Jayasekara et al. (2023)
2 other articles

1 mention without citation

Recent advances in the biodegradation of polyethylene terephthalate with cutinase-like enzymes.
Sui et al. (2023)