› 3hbu

X-ray diffraction
1.77Å resolution

PrtC methionine mutants: M226H DESY

Released:
DOI: 10.2210/pdb3hbu/pdb
PDB entry 3hbu coloured by chain, front view.
PDB entry 3hbu coloured by chain, side view.
PDB entry 3hbu coloured by chain, top view.
Source organisms:
Primary publication:
Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site.
Oberholzer AE, Bumann M, Hege T, Russo S, Baumann U
Biol Chem 390 875-81 (2009)
PMID: 19558324

Function and Biology Details

Reaction catalysed: 
Preferential cleavage of bonds with hydrophobic residues in P1'.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147683 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serralysin C Chain: P
Molecule details ›
Chain: P
Length: 462 amino acids
Theoretical weight: 49.77 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
  • Canonical: P16317 (Residues: 18-479; Coverage: 97%)
Gene name: prtC
Sequence domains:
Structure domains:
peptide Chain: Z
Molecule details ›
Chain: Z
Length: 4 amino acids
Theoretical weight: 360 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand CA 7 x CA
Ligand ZN 3 x ZN
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3121
Unit cell:
a: 102.112Å b: 102.112Å c: 122.863Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.166 0.187
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

4 review citations

Architecture and function of metallopeptidase catalytic domains.
Cerdà-Costa et al. (2014)
3 more