› 6ix8

X-ray diffraction
1.66Å resolution

The structure of LepI C52A in complex with SAM and its substrate analogue

Released:
DOI: 10.2210/pdb6ix8/pdb
Model geometry
Fit model/data
PDB entry 6ix8 coloured by chain, front view.
PDB entry 6ix8 coloured by chain, side view.
PDB entry 6ix8 coloured by chain, top view.
Source organism: Aspergillus flavus NRRL3357
Primary publication:
Structural basis for stereoselective dehydration and hydrogen-bonding catalysis by the SAM-dependent pericyclase LepI.
Cai Y, Hai Y, Ohashi M, Jamieson CS, Garcia-Borras M, Houk KN, Zhou J, Tang Y
OpenAccess logo Nat Chem 11 812-820 (2019)
PMID: 31332284

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110750 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-methyltransferase lepI Chains: A, B
Molecule details ›
Chains: A, B
Length: 405 amino acids
Theoretical weight: 45.46 KDa
Source organism: Aspergillus flavus NRRL3357
Expression system: Escherichia coli
UniProt:
  • Canonical: B8NJH3 (Residues: 2-387; Coverage: 100%)
Gene names: AFLA_066940, lepI
Sequence domains: O-methyltransferase domain

Ligands and Environments

6 bound ligands:
Ligand SAM 2 x SAM
Ligand CL 4 x CL
Ligand NA 3 x NA
Ligand B3O 2 x B3O
Ligand EDO 4 x EDO
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: C2
Unit cell:
a: 160.8Å b: 62.562Å c: 113.836Å
α: 90° β: 113.34° γ: 90°
R-values:
R R work R free
0.169 0.168 0.197
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Diversity of the reaction mechanisms of SAM-dependent enzymes.
Sun et al. (2021)
4 more

2 mentions without citation

Structural basis for stereoselective dehydration and hydrogen-bonding catalysis by the SAM-dependent pericyclase LepI.
Cai et al. (2019)
1 more