› 4dnm

X-ray diffraction
2.15Å resolution

Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound hepes, space group p3221

Released:
DOI: 10.2210/pdb4dnm/pdb
PDB entry 4dnm coloured by chain, front view.
PDB entry 4dnm coloured by chain, side view.
PDB entry 4dnm coloured by chain, top view.
Source organism: Burkholderia multivorans ATCC 17616
Entry authors: Vetting MW, Toro R, Bhosle R, Seidel RD, Hillerich B, Washington E, Scott Glenn A, Chowdhury S, Evans B, Hammonds J, Al Obaidi NF, Zencheck WD, Imker HJ, Gerlt JA, Raushel FM, Almo SC, Enzyme Function Initiative (EFI)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-fucono-1,5-lactonase Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 33.96 KDa
Source organism: Burkholderia multivorans ATCC 17616
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3KNC4 (Residues: 1-296; Coverage: 100%)
Gene name: BMULJ_04915
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
Ligand GOL 3 x GOL
Ligand ZN 1 x ZN
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3221
Unit cell:
a: 75.07Å b: 75.07Å c: 142.26Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.228
Expression system: Escherichia coli BL21(DE3)

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