› 1trl

Solution NMR

NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316 OF THERMOLYSIN: A DIMER FORMED BY SUBUNITS HAVING THE NATIVE STRUCTURE

Released:
DOI: 10.2210/pdb1trl/pdb
PDB entry 1trl coloured by chain, ensemble of 8 models, front view.
PDB entry 1trl coloured by chain, ensemble of 8 models, side view.
PDB entry 1trl coloured by chain, ensemble of 8 models, top view.
Source organism: Bacillus thermoproteolyticus
Primary publication:
NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure.
Rico M, Jiménez MA, González C, De Filippis V, Fontana A
Biochemistry 33 14834-47 (1994)
PMID: 7993910

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: -|-Leu > -|-Phe.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 62 amino acids
Theoretical weight: 6.63 KDa
Source organism: Bacillus thermoproteolyticus
Expression system: Not provided
UniProt:
  • Canonical: P00800 (Residues: 487-548; Coverage: 12%)
Gene name: npr
Sequence domains: Thermolysin metallopeptidase, alpha-helical domain
Structure domains: Neutral Protease Domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

8 citation in other articles

A rapid test for identification of autonomous folding units in proteins.
Fischer et al. (2000)
7 more

11 mentions without citation

An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state.
Zhang et al. (2004)
10 more