7JMQ

The external aldimine form of the mutant beta-S377A Salmonella thypi tryptophan synthase in open conformation showing dual side chain conformations for the residue beta-Q114, sodium ion at the metal coordination site, and F9 inhibitor at the alpha-site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (A)	Tryptophan synthase alpha chain	polymer	268	28698.8	1	UniProt (P00929) Pfam (PF00290)	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
2	B (B)	Tryptophan synthase beta chain	polymer	397	42902.9	1	UniProt (P0A2K1) Pfam (PF00291)	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
3	AA, BA, C, CA, D... (B, A)	DIMETHYL SULFOXIDE	non-polymer		78.1	33	Chemie (DMS)
4	J (A)	2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL DIHYDROGEN PHOSPHATE	non-polymer		365.2	1	Chemie (F9F)
5	O, QA (A, B)	CESIUM ION	non-polymer		132.9	2	Chemie (CS)
6	U (B)	(E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine	non-polymer		334.2	1	Chemie (KOU)
7	DA, EA (B)	GLYCEROL	non-polymer		92.1	2	Chemie (GOL)
8	HA, LA (B)	1,2-ETHANEDIOL	non-polymer		62.1	2	Chemie (EDO)
9	RA (B)	SODIUM ION	non-polymer		23.0	1	Chemie (NA)
10	SA (B)	CHLORIDE ION	non-polymer		35.5	1	Chemie (CL)
11	TA, UA (A, B)	water	water		18.0	794	Chemie (HOH)

Sequence modifications

B: 1 - 397 (UniProt: P0A2K1)

PDB	External Database	Details
Ala 377	Ser 377	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	71601.7
Non-Polymers*	Number of molecules	43
	Total formula weight	3910.4
All*	Total formula weight	75512.1

*Water molecules are not included.