5A6S

Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (A)	ENDOLYSIN	polymer	294	32877.2	1	UniProt (D9ZNF3)	CLOSTRIDIUM PHAGE PHICTP1
2	B (B)	ENDOLYSIN	polymer	80	9031.1	1	UniProt (D9ZNF3)	CLOSTRIDIUM PHAGE PHICTP1
3	C (A)	SULFATE ION	non-polymer		96.1	1	Chemie (SO4)
4	D, E, G (A, B)	GLYCEROL	non-polymer		92.1	3	Chemie (GOL)
5	F (A)	PENTAETHYLENE GLYCOL	non-polymer		238.3	1	Chemie (1PE)
6	H, I (A, B)	water	water		18.0	480	Chemie (HOH)

Sequence modifications

A: 1 - 274 (UniProt: D9ZNF3)

PDB	External Database	Details
Met -19	-	expression tag
Gly -18	-	expression tag
Ser -17	-	expression tag
Ser -16	-	expression tag
His -15	-	expression tag
His -14	-	expression tag
His -13	-	expression tag
His -12	-	expression tag
His -11	-	expression tag
His -10	-	expression tag
Ser -9	-	expression tag
Ser -8	-	expression tag
Gly -7	-	expression tag
Leu -6	-	expression tag
Val -5	-	expression tag
Pro -4	-	expression tag
Arg -3	-	expression tag
Gly -2	-	expression tag
Ser -1	-	expression tag
His 0	-	expression tag

B: 195 - 274 (UniProt: D9ZNF3)

PDB	External Database	Details
Met 195	Val 195	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	41908.3
Non-Polymers*	Number of molecules	5
	Total formula weight	610.6
All*	Total formula weight	42518.9

*Water molecules are not included.