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PDBe Entry: 1dku view

CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 19.8%, Free R-factor: 24.1%, Spacegroup: P 63
Released 05/04/2000, deposition: 08/12/1999, last revision: 24/02/2009
Authors Eriksen, T.A.search; Kadziola, A.search; Bentsen, A.-K.search; Harlow, K.W.search; Larsen, S.search
Primary citation Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase.
NAT.STRUCT.BIOL.search vol:7, pag:303-308 (2000) [PubMed ID 10742175 ]search
Keywords OPEN ALPHA-BETA STRUCTUREsearch, DOMAIN DUPLICATIONsearch, PHOSPHORIBOSYLTRANSFERASE TYPE I FOLDsearch
EC 2.7.6.1 ExPASy BRENDA search (A B)
Organism Bacillus subtilis 1423search(A B)
UniProt Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) (RPPK) (Phosphoribosyl pyrophosphate synthetase) (P-Rib-PP synthetase) (PRPP synthetase) P14193search (A B)
Solvent A, B
Related entries 1dkr
Polymers
Id Name Type UniProt Residues Observed
A, B PROTEIN (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE) Protein P14193 (KPRS_BACSU)search
 317 93%
Heterogens
Id Name Ligands
B, A PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER AP2 search
A, B METHYL PHOSPHONIC ACID ADENOSINE ESTER ABM search
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