3ugv

X-ray diffraction
2.3Å resolution

Crystal structure of an enolase from alpha pretobacterium bal199 (EFI TARGET EFI-501650) with bound MG

Released:
Source organism: alpha proteobacterium BAL199
Entry authors: Vetting MW, Toro R, Bhosle R, Wasserman SR, Morisco LL, Hillerich B, Washington E, Scott Glenn A, Chowdhury S, Evans B, Hammonds J, Zencheck WD, Imker HJ, Gerlt JA, Almo SC, Enzyme Function Initiative (EFI)

Function and Biology Details

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MR_MLE domain-containing protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 390 amino acids
Theoretical weight: 42.94 KDa
Source organism: alpha proteobacterium BAL199
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A8TYI5 (Residues: 1-367; Coverage: 100%)
Gene name: BAL199_22462
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P212121
Unit cell:
a: 152.711Å b: 152.984Å c: 173.535Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.16 0.208
Expression system: Escherichia coli BL21(DE3)