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PDBe Entry: 1i7q view

ANTHRANILATE SYNTHASE FROM S. MARCESCENS
Summary
Header LYASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.95 Å, R-factor: 18.1%, Free R-factor: 24.6%, Spacegroup: P 1 21 1
Released 16/05/2001, deposition: 10/03/2001, last revision: 24/02/2009
Authors Spraggon, G.search; Kim, C.search; Nguyen-Huu, X.search; Yee, M.-C.search; Yanofsky, C.search; Mills, S.E.search
Primary citation The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
PROC.NATL.ACAD.SCI.USAsearch vol:98, pag:6021-6026 (2001) [PubMed ID 11371633 ]search
Keywords ANTHRANILATE SYNTHASEsearch, GLUTAMYL THIOESTERsearch, ANTHRANILATE BIOSYNTHESISsearch, CHORISMATE BINDINGsearch, LYASEsearch
EC 4.1.3.27 ExPASy BRENDA search (A B C D)
Organism Serratia marcescens 615search(A C B D)
UniProt Anthranilate synthase component 1 (EC 4.1.3.27) (Anthranilate synthase component I) P00897search (A C)
Anthranilate synthase component II (EC 4.1.3.27) (Glutamine amido-transferase) P00900search (B D)
Solvent A, B, C, D
Polymers
Id Name Type UniProt Residues Observed
A, C ANTHRANILATE SYNTHASE Protein P00897 (TRPE_SERMA)search
519 99%
B, D TRPG Protein P00900 (TRPG_SERMA)search
193 99%
Heterogens
Id Name Ligands
A, C MAGNESIUM ION MG search
B, D GLUTAMYL GROUP ILG search
A, C BENZOIC ACID BEZ search
A, C PYRUVIC ACID PYR search
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