› 3znu

X-ray diffraction
1.65Å resolution

Crystal structure of ClcF in crystal form 2

Released:
DOI: 10.2210/pdb3znu/pdb
PDB entry 3znu coloured by chain, front view.
PDB entry 3znu coloured by chain, side view.
PDB entry 3znu coloured by chain, top view.
Source organism: Rhodococcus opacus
Primary publication:
Crystal structure and catalytic mechanism of chloromuconolactone dehalogenase ClcF from Rhodococcus opacus 1CP.
Roth C, Gröning JA, Kaschabek SR, Schlömann M, Sträter N
Mol Microbiol 88 254-67 (2013)
PMID: 23421784

Function and Biology Details

Reaction catalysed: 
(+)-muconolactone = 5-oxo-4,5-dihydrofuran-2-acetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Muconolactone Delta-isomerase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 94 amino acids
Theoretical weight: 11.21 KDa
Source organism: Rhodococcus opacus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8G9L0 (Residues: 1-94; Coverage: 100%)
Gene names: R1CP_39625, clcF
Sequence domains: Muconolactone delta-isomerase
Structure domains: Dimeric alpha+beta barrel

Ligands and Environments

3 bound ligands:
Ligand CL 14 x CL
Ligand EDO 21 x EDO
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P212121
Unit cell:
a: 78.242Å b: 103.574Å c: 141.667Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.191
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Evolutionary relationships between heme-binding ferredoxin α + β barrels.
Acharya et al. (2016)

3 mentions without citation

Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme.
Celis et al. (2015)
2 more