› 2jug

Solution NMR

Multienzyme Docking in Hybrid Megasynthetases

Released:
DOI: 10.2210/pdb2jug/pdb
PDB entry 2jug coloured by chain, ensemble of 10 models, front view.
PDB entry 2jug coloured by chain, ensemble of 10 models, side view.
PDB entry 2jug coloured by chain, ensemble of 10 models, top view.
Source organism: Archangium disciforme
Primary publication:
Multienzyme docking in hybrid megasynthetases.
Richter CD, Nietlispach D, Broadhurst RW, Weissman KJ
Nat Chem Biol 4 75-81 (2008)
PMID: 18066054

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carrier domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 78 amino acids
Theoretical weight: 8.13 KDa
Source organism: Archangium disciforme
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5ZPA9 (Residues: 2-74; Coverage: 3%)
Gene name: tubC
Sequence domains: TubC N-terminal docking domain
Structure domains: Non-ribosomal peptide synthase, adenylation domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

20 review citations

Nonribosomal Peptide Synthesis-Principles and Prospects.
Süssmuth et al. (2017)
19 more

1 mention without citation

Structural elements of an NRPS cyclization domain and its intermodule docking domain.
Dowling et al. (2016)