› 1thf

X-ray diffraction
1.45Å resolution

CYCLASE SUBUNIT OF IMIDAZOLEGLYCEROLPHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA

Released:
DOI: 10.2210/pdb1thf/pdb
PDB entry 1thf coloured by chain, front view.
PDB entry 1thf coloured by chain, side view.
PDB entry 1thf coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion.
Lang D, Thoma R, Henn-Sax M, Sterner R, Wilmanns M
Science 289 1546-50 (2000)
PMID: 10968789

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazole glycerol phosphate synthase subunit HisF Chain: D
Molecule details ›
Chain: D
Length: 253 amino acids
Theoretical weight: 27.74 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0C6 (Residues: 1-253; Coverage: 100%)
Gene names: TM_1036, hisF
Sequence domains: Histidine biosynthesis protein
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: C2
Unit cell:
a: 79.68Å b: 44.42Å c: 63.91Å
α: 90° β: 112.01° γ: 90°
R-values:
R R work R free
0.198 0.178 0.214
Expression system: Escherichia coli

Quick links

Citations

28 review citations

One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.
Nagano et al. (2002)
27 more

26 mentions without citation

Why reinvent the wheel? Building new proteins based on ready-made parts.
Khersonsky et al. (2016)
25 more