› 4d56

X-ray diffraction
2.1Å resolution

Understanding bi-specificity of A-domains

Released:
DOI: 10.2210/pdb4d56/pdb
PDB entry 4d56 coloured by chain, front view.
PDB entry 4d56 coloured by chain, side view.
PDB entry 4d56 coloured by chain, top view.
Source organism: Planktothrix agardhii
Primary publication:
Structural Elucidation of the Bispecificity of A Domains as a Basis for Activating Non-natural Amino Acids.
Kaljunen H, Schiefelbein SH, Stummer D, Kozak S, Meijers R, Christiansen G, Rentmeister A
Angew Chem Int Ed Engl 54 8833-6 (2015)
PMID: 26096082

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-515116 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ApnAA1 Chain: A
Molecule details ›
Chain: A
Length: 573 amino acids
Theoretical weight: 64.59 KDa
Source organism: Planktothrix agardhii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: G0WVH3 (Residues: 1-547; Coverage: 100%)
Gene name: apnA
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand TYR 1 x TYR
Ligand PO4 2 x PO4
Ligand GOL 1 x GOL
Ligand AMP 1 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P212121
Unit cell:
a: 68.166Å b: 82.242Å c: 90.064Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.223
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

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

1 mention without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)