› 5bk7

X-ray diffraction
2.2Å resolution

The structure of MppP E15A mutant soaked with the substrate L-arginine

Released:
DOI: 10.2210/pdb5bk7/pdb
PDB entry 5bk7 coloured by chain, front view.
PDB entry 5bk7 coloured by chain, side view.
PDB entry 5bk7 coloured by chain, top view.
Source organism: Streptomyces wadayamensis
Primary publication:
Streptomyces wadayamensis MppP is a PLP-Dependent Oxidase, Not an Oxygenase.
Han L, Vuksanovic N, Oehm SA, Fenske TG, Schwabacher AW, Silvaggi NR
Biochemistry 57 3252-3264 (2018)
PMID: 29473729

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class I/classII domain-containing protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 376 amino acids
Theoretical weight: 41.48 KDa
Source organism: Streptomyces wadayamensis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0X1KHF5 (Residues: 1-376; Coverage: 100%)
Sequence domains: Aminotransferase class I and II

Ligands and Environments

1 bound ligand:
Ligand EQJ 8 x EQJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 64.441Å b: 200.514Å c: 139.93Å
α: 90° β: 103.25° γ: 90°
R-values:
R R work R free
0.202 0.201 0.258
Expression system: Escherichia coli

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Citations

3 review citations

Pyridoxal phosphate-dependent reactions in the biosynthesis of natural products.
Du et al. (2019)
2 more