2VEK

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

Summary for 2VEK

Entry DOI	10.2210/pdb2vek/pdb
Related	1AG1 1DKW 1IIG 1IIH 1KV5 1ML1 1MSS 1MTM 1TPD 1TPE 1TPF 1TRD 1TRI 1TSI 1TTI 1TTJ 2J24 2J27 2V0T 2V2C 2V2D 2V2H 2V5L 2VEI 2VEL 2VEM 2VEN 3TIM 4TIM 5TIM 6TIM
Descriptor	TRIOSEPHOSPHATE ISOMERASE, CITRIC ACID, TERTIARY-BUTYL ALCOHOL, ... (5 entities in total)
Functional Keywords	isomerase, triosephosphate isomerase, tim barrel, glycolysis, engineering, pentose shunt, binding pocket, gluconeogenesis, lipid synthesis, substrate specificity, fatty acid biosynthesis, tim, enzyme, monomeric, glycosome
Biological source	TRYPANOSOMA BRUCEI BRUCEI
Cellular location	Glycosome: P04789
Total number of polymer chains	2
Total formula weight	51971.20
Authors	Alahuhta, M.,Salin, M.,Casteleijn, M.G.,Kemmer, C.,El-Sayed, I.,Augustyns, K.,Neubauer, P.,Wierenga, R.K. (deposition date: 2007-10-24, release date: 2008-02-19, Last modification date: 2023-12-13)
Primary citation	Alahuhta, M.,Salin, M.,Casteleijn, M.G.,Kemmer, C.,El-Sayed, I.,Augustyns, K.,Neubauer, P.,Wierenga, R.K. Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21:257-, 2008 Cited by PubMed: 18239072 DOI: 10.1093/PROTEIN/GZN002 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation