3FNM

Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, C (A, C)	Gamma-glutamyltranspeptidase (Ggt) Large subunit	polymer	377	40577.4	2	UniProt (O25743) Pfam (PF01019)	Helicobacter pylori (Campylobacter pylori)
2	B, D (B, D)	Gamma-glutamyltranspeptidase (Ggt) Small subunit	polymer	188	20410.2	2	UniProt (O25743) Pfam (PF01019)	Helicobacter pylori (Campylobacter pylori)
3	E, F (B, D)	(2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID	non-polymer		178.6	2	Chemie (AVN)
4	G, H, I, J (A, B, C, D)	water	water		18.0	534	Chemie (HOH)

Sequence modifications

A, C: 25 - 379 (UniProt: O25743)

PDB	External Database	Details
Met 3	-	expression tag
Gly 4	-	expression tag
Ser 5	-	expression tag
Ser 6	-	expression tag
His 7	-	expression tag
His 8	-	expression tag
His 9	-	expression tag
His 10	-	expression tag
His 11	-	expression tag
His 12	-	expression tag
Ser 13	-	expression tag
Ser 14	-	expression tag
Gly 15	-	expression tag
Leu 16	-	expression tag
Val 17	-	expression tag
Pro 18	-	expression tag
Arg 19	-	expression tag
Gly 20	-	expression tag
Ser 21	-	expression tag
His 22	-	expression tag
Met 23	-	expression tag
Ala 24	-	expression tag

Contents of the asymmetric unit

Polymers	Number of chains	4
	Total formula weight	121975.1
Non-Polymers*	Number of molecules	2
	Total formula weight	357.1
All*	Total formula weight	122332.3

*Water molecules are not included.