1jcm

X-ray diffraction
2.1Å resolution

TRPC STABILITY MUTANT CONTAINING AN ENGINEERED DISULPHIDE BRIDGE AND IN COMPLEX WITH A CDRP-RELATED SUBSTRATE

Released:

Function and Biology Details

Reactions catalysed:
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O
N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
PDBe Complex ID:
PDB-CPX-133677 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan biosynthesis protein TrpCF Chain: P
Molecule details ›
Chain: P
Length: 259 amino acids
Theoretical weight: 28.92 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00909 (Residues: 2-260; Coverage: 57%)
Gene names: JW1254, b1262, trpC, trpF
Sequence domains: Indole-3-glycerol phosphate synthase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P6322
Unit cell:
a: 81.638Å b: 81.638Å c: 156.745Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.241 0.241 0.319
Expression system: Escherichia coli BL21(DE3)