2VEL

Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A, B	GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE	polymer	238	25659.3	2	UniProt (P04789) Pfam (PF00121) In PDB	TRYPANOSOMA BRUCEI BRUCEI	TIM, TRIOSE-PHOSPHATE ISOMERASE, TRIOSEPHOSPHATE ISOMERASE
2	A, B	CHLORIDE ION	non-polymer		35.5	2	Chemie (CL)
3	A, B	2-PHOSPHOGLYCOLIC ACID	non-polymer		156.0	2	Chemie (PGA)
4		water	water		18.0	356	Chemie (HOH)

Sequence modifications

A, B: 15 - 72 (UniProt: P04789)

PDB	External Database	Details
Ser 15	Asn 15	conflict
Pro 18	Gln 18	conflict
Asp 19	Gln 19	conflict
Gly 68	Ile 68	conflict
Asn 69	Ala 69	conflict
Ala 70	Lys 70	conflict
Asp 71	Ser 71	conflict
Ala 72	Gly 72	conflict

A, B: 80 - 234 (UniProt: P04789)

PDB	External Database	Details
Ala 81	Pro 81	conflict
Ser 82	Ile 82	conflict
Trp 100	Ala 100	conflict
Ala 233	Val 233	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	2
	Total formula weight	51318.6
Non-Polymers*	Number of molecules	4
	Total formula weight	383.0
All*	Total formula weight	51701.5

*Water molecules are not included.