› 1ef9

X-ray diffraction
2.7Å resolution

THE CRYSTAL STRUCTURE OF METHYLMALONYL COA DECARBOXYLASE COMPLEXED WITH 2S-CARBOXYPROPYL COA

Released:
DOI: 10.2210/pdb1ef9/pdb
PDB entry 1ef9 coloured by chain, front view.
PDB entry 1ef9 coloured by chain, side view.
PDB entry 1ef9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli.
Benning MM, Haller T, Gerlt JA, Holden HM
Biochemistry 39 4630-9 (2000)
PMID: 10769118

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156458 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylmalonyl-CoA decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 29.21 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P52045 (Residues: 1-261; Coverage: 100%)
Gene names: JW2886, b2919, mmcD, scpB, ygfG
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 2CP 1 x 2CP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 85.7Å b: 142.4Å c: 89.7Å
α: 90° β: 109.2° γ: 90°
R-values:
R R work R free
0.19 not available not available

Quick links

Citations

10 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
9 more

2 mentions without citation

Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core.
Hall et al. (2003)
1 more