› 3mah

X-ray diffraction
2.31Å resolution

A putative c-terminal regulatory domain of aspartate kinase from porphyromonas gingivalis w83.

Released:
DOI: 10.2210/pdb3mah/pdb
PDB entry 3mah coloured by chain, front view.
PDB entry 3mah coloured by chain, side view.
PDB entry 3mah coloured by chain, top view.
Source organism: Porphyromonas gingivalis W83
Entry authors: Filippova EV, Minasov G, Shuvalova L, Kiryukhina O, Moy S, Joachimiak A, Anderson FW, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed: 
ATP + L-aspartate = ADP + 4-phospho-L-aspartate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartokinase Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.63 KDa
Source organism: Porphyromonas gingivalis W83
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7MT13 (Residues: 290-446; Coverage: 35%)
Gene names: PG_2189, lysC
Sequence domains: ACT domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P6522
Unit cell:
a: 46.67Å b: 46.67Å c: 221.902Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.211 0.24
Expression system: Escherichia coli BL21

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