› 5nj9

X-ray diffraction
1.25Å resolution

E. coli Microcin-processing metalloprotease TldD/E with DRVY angiotensin fragment bound

Released:
DOI: 10.2210/pdb5nj9/pdb
PDB entry 5nj9 coloured by chain, front view.
PDB entry 5nj9 coloured by chain, side view.
PDB entry 5nj9 coloured by chain, top view.
Source organisms:
Primary publication:
The Origins of Specificity in the Microcin-Processing Protease TldD/E.
Ghilarov D, Serebryakova M, Stevenson CEM, Hearnshaw SJ, Volkov DS, Maxwell A, Lawson DM, Severinov K
Structure 25 1549-1561.e5 (2017)
PMID: 28943336

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-133811 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Metalloprotease TldD Chains: A, C
Molecule details ›
Chains: A, C
Length: 495 amino acids
Theoretical weight: 53.09 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AGG8 (Residues: 1-481; Coverage: 100%)
Gene names: JW3213, b3244, tldD, yhdO
Sequence domains:
Metalloprotease PmbA Chains: B, D
Molecule details ›
Chains: B, D
Length: 450 amino acids
Theoretical weight: 48.42 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AFK0 (Residues: 1-450; Coverage: 100%)
Gene names: JW4194, b4235, pmbA, tldE
Sequence domains:
Structure domains: PmbA/TldD superfamily
Angiotensin 1-4 Chains: E, F
Molecule details ›
Chains: E, F
Length: 4 amino acids
Theoretical weight: 553 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01019 (Residues: 25-28; Coverage: 1%)
Gene names: AGT, SERPINA8

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand MES 4 x MES
Ligand EDO 10 x EDO
Ligand NA 4 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 64.63Å b: 173.53Å c: 82.86Å
α: 90° β: 90.03° γ: 90°
R-values:
R R work R free
0.151 0.149 0.182
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

4 review citations

New developments in RiPP discovery, enzymology and engineering.
Montalbán-López et al. (2021)
3 more

1 mention without citation

The Origins of Specificity in the Microcin-Processing Protease TldD/E.
Ghilarov et al. (2017)