2VSU

A ternary complex of Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) with acetyl-Coenzyme A and vanillin gives insights into substrate specificity and mechanism.

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B, D (A, B, D)	P-HYDROXYCINNAMOYL COA HYDRATASE/LYASE	polymer	276	31028.6	3	UniProt (O69762) Pfam (PF00378)	PSEUDOMONAS FLUORESCENS	HYDROXYCINNAMOYL-COA HYDRATASE-LYASE S123A MUTANT
2	C (C)	P-HYDROXYCINNAMOYL COA HYDRATASE/LYASE	polymer	275	30899.5	1	UniProt (O69762) Pfam (PF00378)	PSEUDOMONAS FLUORESCENS	HYDROXYCINNAMOYL-COA HYDRATASE-LYASE S123A MUTANT
3	E (E)	P-HYDROXYCINNAMOYL COA HYDRATASE/LYASE	polymer	276	31005.6	1	UniProt (O69762) Pfam (PF00378)	PSEUDOMONAS FLUORESCENS	HYDROXYCINNAMOYL-COA HYDRATASE-LYASE S123A MUTANT
4	F (F)	P-HYDROXYCINNAMOYL COA HYDRATASE/LYASE	polymer	276	31056.6	1	UniProt (O69762) Pfam (PF00378)	PSEUDOMONAS FLUORESCENS	HYDROXYCINNAMOYL-COA HYDRATASE-LYASE S123A MUTANT
5	G, H, I, K, L (A, B, D, E, F)	ACETYL COENZYME *A	non-polymer		809.6	5	Chemie (ACO)
6	J (D)	4-hydroxy-3-methoxybenzaldehyde	non-polymer		152.1	1	Chemie (V55)
7	M, N, O, P, Q... (A, B, C, D, E...)	water	water		18.0	488	Chemie (HOH)

Sequence modifications

A, B, D: 1 - 276 (UniProt: O69762)

PDB	External Database	Details
Ala 123	Ser 123	engineered mutation

C: 1 - 250 (UniProt: O69762)

PDB	External Database	Details
Ala 123	Ser 123	engineered mutation

E: 1 - 276 (UniProt: O69762)

PDB	External Database	Details
Ala 123	Ser 123	engineered mutation
Tyr 146	Trp 146	conflict

F: 1 - 276 (UniProt: O69762)

PDB	External Database	Details
Ala 123	Ser 123	engineered mutation
Arg 29	Lys 29	conflict

Contents of the asymmetric unit

Polymers	Number of chains	6
	Total formula weight	186047.5
Non-Polymers*	Number of molecules	6
	Total formula weight	4200.0
All*	Total formula weight	190247.5

*Water molecules are not included.