› 6ms8

X-ray diffraction
1.9Å resolution

Crystal Structure of Chalcone Isomerase from Medicago Truncatula Complexed with (2S) Naringenin

Released:
DOI: 10.2210/pdb6ms8/pdb
Model geometry
Fit model/data
PDB entry 6ms8 coloured by chain, front view.
PDB entry 6ms8 coloured by chain, side view.
PDB entry 6ms8 coloured by chain, top view.
Source organism: Medicago truncatula
Primary publication:
Bifunctional Substrate Activation via an Arginine Residue Drives Catalysis in Chalcone Isomerases
Burke JR, La Clair JJ, Philippe RN, Pabis A, Jez JM, Cortina G, Kaltenbach M, Bowman ME, Woods KB, Nelson AT, Tawfik DS, Kamerlin SCL, Noel JP
ACS Catalysis (2019)

Function and Biology Details

Reaction catalysed: 
A chalcone = a flavanone
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chalcone-flavonone isomerase family protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 224 amino acids
Theoretical weight: 24.36 KDa
Source organism: Medicago truncatula
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B7FJK3 (Residues: 1-224; Coverage: 100%)
Gene names: 11445536, MTR_1g115870
Sequence domains: Chalcone-flavanone isomerase

Ligands and Environments

1 bound ligand:
Ligand NAR 5 x NAR
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P32
Unit cell:
a: 85.09Å b: 85.09Å c: 221.508Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.228 0.241
Expression system: Escherichia coli BL21(DE3)

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