› 1t4a

X-ray diffraction
2Å resolution

Structure of B. Subtilis PurS C2 Crystal Form

Released:
DOI: 10.2210/pdb1t4a/pdb
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PDB entry 1t4a coloured by chain, front view.
PDB entry 1t4a coloured by chain, side view.
PDB entry 1t4a coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
A model for the Bacillus subtilis formylglycinamide ribonucleotide amidotransferase multiprotein complex.
Anand R, Hoskins AA, Bennett EM, Sintchak MD, Stubbe J, Ealick SE
Biochemistry 43 10343-52 (2004)
PMID: 15301532

Function and Biology Details

Reaction 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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146085 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylformylglycinamidine synthase subunit PurS Chains: A, B
Molecule details ›
Chains: A, B
Length: 84 amino acids
Theoretical weight: 9.95 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12049 (Residues: 1-84; Coverage: 100%)
Gene names: BSU06460, purS, yexA
Sequence domains: Phosphoribosylformylglycinamidine (FGAM) synthase
Structure domains: Phosphoribosylformylglycinamidine synthase subunit PurS

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 8-BM
Spacegroup: C2
Unit cell:
a: 89.128Å b: 42.206Å c: 47.033Å
α: 90° β: 118.22° γ: 90°
R-values:
R R work R free
0.217 0.213 0.283
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
3 more

2 mentions without citation

The JCSG MR pipeline: optimized alignments, multiple models and parallel searches.
Schwarzenbacher et al. (2008)
1 more

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