3d54

X-ray diffraction
3.5Å resolution

Structure of PurLQS from Thermotoga maritima

Released:

Function and Biology Details

Reactions catalysed:
ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate
L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-194750 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Phosphoribosylformylglycinamidine synthase subunit PurL Chains: A, E, I
Phosphoribosylformylglycinamidine synthase subunit PurS Chains: B, C, F, G, J, K
Molecule details ›
Chains: B, C, F, G, J, K
Length: 82 amino acids
Theoretical weight: 9.66 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0X1 (Residues: 1-82; Coverage: 100%)
Gene names: THEMA_08115, TM_1244, Tmari_1249, purS
Sequence domains: Phosphoribosylformylglycinamidine (FGAM) synthase
Structure domains: Phosphoribosylformylglycinamidine synthase subunit PurS
Phosphoribosylformylglycinamidine synthase subunit PurQ Chains: D, H, L
Molecule details ›
Chains: D, H, L
Length: 213 amino acids
Theoretical weight: 23.75 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0X2 (Residues: 1-213; Coverage: 100%)
Gene names: TM_1245, purQ
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 256.851Å b: 187.337Å c: 159.177Å
α: 90° β: 99.12° γ: 90°
R-values:
R R work R free
0.252 0.252 0.282
Expression system: Escherichia coli