› 2tmg

X-ray diffraction
2.9Å resolution

THERMOTOGA MARITIMA GLUTAMATE DEHYDROGENASE MUTANT S128R, T158E, N117R, S160E

Released:
DOI: 10.2210/pdb2tmg/pdb
PDB 2tmg coloured by chain and viewed from the front.
PDB 2tmg coloured by chain and viewed from the side.
PDB 2tmg coloured by chain and viewed from the top.
Source organism: Thermotoga maritima
Primary publication:
Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface.
Lebbink JH, Knapp S, van der Oost J, Rice D, Ladenstein R, de Vos WM
J. Mol. Biol. 289 357-69 (1999)
PMID: 10366510

Function and Biology Details

Reaction catalysed: 
L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate dehydrogenase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 415 amino acids
Theoretical weight: 45.91 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P96110 (Residues: 2-416; Coverage: 100%)
Gene names: TM_1015, gdh, gdhA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3121
Unit cell:
a: 145.1Å b: 145.1Å c: 272.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.211 0.274
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Rational engineering of enzyme stability.
Eijsink et al. (2004)
3 more