› 6r7v

X-ray diffraction
1.4Å resolution

Tannerella forsythia promirolysin mutant E225A

Released:
DOI: 10.2210/pdb6r7v/pdb
PDB entry 6r7v coloured by chain, front view.
PDB entry 6r7v coloured by chain, side view.
PDB entry 6r7v coloured by chain, top view.
Source organism: Tannerella forsythia
Primary publication:
Structure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases.
Guevara T, Rodriguez-Banqueri A, Ksiazek M, Potempa J, Gomis-Rüth FX
IUCrJ 7 18-29 (2020)
PMID: 31949901

Function and Biology Details

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-124639 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Karilysin Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 35.38 KDa
Source organism: Tannerella forsythia
Expression system: Escherichia coli
UniProt:
  • Canonical: G8ULV1 (Residues: 20-331; Coverage: 51%)
Gene name: BFO_2661
Sequence domains: Pregnancy-associated plasma protein-A

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand ZN 1 x ZN
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 47.33Å b: 67.25Å c: 79.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 0.188
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism.
Kobberø et al. (2022)
3 more

4 mentions without citation

Structure-based mechanism of cysteine-switch latency and of catalysis by pappalysin-family metallopeptidases.
Guevara et al. (2020)
3 more