› 7lce

X-ray diffraction
2.58Å resolution

Function and Biology Details

Reaction catalysed: 
2-amino-2-deoxy-D-gluconate 6-phosphate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-glucosaminate-6-phosphate ammonia lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 369 amino acids
Theoretical weight: 39.59 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: D0ZLR3 (Residues: 1-369; Coverage: 100%)
Gene names: STM14_4544, dgaE
Sequence domains: L-seryl-tRNA selenium transferase

Ligands and Environments

2 bound ligands:
Ligand DMS 6 x DMS
Ligand CA 16 x CA
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P2221
Unit cell:
a: 60.374Å b: 171.569Å c: 195.054Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.229
Expression system: Escherichia coli

Quick links

Citations

2 mentions without citation

Structure and Mechanism of d-Glucosaminate-6-phosphate Ammonia-lyase: A Novel Octameric Assembly for a Pyridoxal 5'-Phosphate-Dependent Enzyme, and Unprecedented Stereochemical Inversion in the Elimination Reaction of a d-Amino Acid.
Phillips et al. (2021)
1 more

PDB-REDO

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