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3nqz

X-ray diffraction
2.05Å resolution

Crystal structure of the autoprocessed Vibriolysin MCP-02 with E369A mutation

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
Preferential cleavage of bonds with bulky hydrophobic groups in P2 andP1'. Phe at P1' is the most favored residue, which distinguished thisenzyme from thermolysin.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-106589 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Secreted metalloprotease Mcp02 Chain: A
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 19.78 KDa
Source organism: Pseudoalteromonas sp. SM9913
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A1DRD5 (Residues: 25-204; Coverage: 26%)
Gene name: mcp02
Sequence domains:
Structure domains:
Secreted metalloprotease Mcp02 Chain: B
Molecule details ›
Chain: B
Length: 315 amino acids
Theoretical weight: 33.91 KDa
Source organism: Pseudoalteromonas sp. SM9913
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A1DRD5 (Residues: 205-519; Coverage: 45%)
Gene name: mcp02
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P3221
Unit cell:
a: 82.535Å b: 82.535Å c: 154.206Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.22
Expression system: Escherichia coli BL21(DE3)