› 7b2b

Solution NMR

Solution structure of a non-covalent extended docking domain complex of the Pax NRPS: PaxA T1-CDD/PaxB NDD

Released:
DOI: 10.2210/pdb7b2b/pdb
PDB entry 7b2b coloured by chain, ensemble of 20 models, front view.
PDB entry 7b2b coloured by chain, ensemble of 20 models, side view.
PDB entry 7b2b coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
Cooperation between a T Domain and a Minimal C-Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS.
Watzel J, Duchardt-Ferner E, Sarawi S, Bode HB, Wöhnert J
OpenAccess logo Angew Chem Int Ed Engl 60 14171-14178 (2021)
PMID: 33876501

Function and Biology Details

Reaction catalysed: 
ATP + L-phenylalanine + H(2)O = AMP + diphosphate + D-phenylalanine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104826 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carrier domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 31 amino acids
Theoretical weight: 3.62 KDa
Source organism: Xenorhabdus cabanillasii
Expression system: Escherichia coli BL21(DE3)
UniProt: Gene name: BDD26_3339
Carrier domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.98 KDa
Source organism: Xenorhabdus cabanillasii JM26
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: W1J0W9 (Residues: 981-1084; Coverage: 10%)
Gene names: XCR1_180002, paxA
Sequence domains: Phosphopantetheine attachment site

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Deletion of COM donor and acceptor domains and the interaction between modules in bacillomycin D produced by Bacillus amyloliquefaciens.
Lv et al. (2022)

1 mention without citation

Cooperation between a T Domain and a Minimal C-Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS.
Watzel et al. (2021)