8AQ0

Crystal structure of L-N-Carbamoylase from Sinorhizobium meliloti mutant L217G/F329C

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B (A, B)	N-carbamoyl-L-amino-acid hydrolase	polymer	437	46939.1	2	UniProt (Q6DTN4)	Sinorhizobium meliloti	Hydantoin utilization protein C,L-N-carbamoylase
2	C, E, H, J (A, B)	ZINC ION	non-polymer		65.4	4	Chemie (ZN)
3	D, F, I, K (A, B)	FE (III) ION	non-polymer		55.8	4	Chemie (FE)
4	G, L (A, B)	(2~{S})-2-(aminocarbonylamino)-3-(4-hydroxyphenyl)propanoic acid	non-polymer		224.2	2	Chemie (NV6)
5	M (B)	CHLORIDE ION	non-polymer		35.5	1	Chemie (CL)
6	N, O (A, B)	water	water		18.0	125	Chemie (HOH)

Sequence modifications

A, B: 1 - 416 (UniProt: Q6DTN4)

PDB	External Database	Details
Met -20	-	initiating methionine
Gly -19	-	expression tag
Ser -18	-	expression tag
Ser -17	-	expression tag
His -16	-	expression tag
His -15	-	expression tag
His -14	-	expression tag
His -13	-	expression tag
His -12	-	expression tag
His -11	-	expression tag
Gly -10	-	expression tag
Ser -9	-	expression tag
Gly -8	-	expression tag
Leu -7	-	expression tag
Val -6	-	expression tag
Pro -5	-	expression tag
Arg -4	-	expression tag
Gly -3	-	expression tag
Ser -2	-	expression tag
Ala -1	-	expression tag
Gly 0	-	expression tag
Gly 217	Leu 217	engineered mutation
Cys 329	Phe 329	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	93878.2
Non-Polymers*	Number of molecules	11
	Total formula weight	968.9
All*	Total formula weight	94847.1

*Water molecules are not included.