1FJT

THERMOLYSIN (50% ACETONITRILE SOAKED CRYSTALS)

Summary for 1FJT

• Entry DOI: 10.2210/pdb1fjt/pdb
• Related: 1FJ3 1FJO 1FJQ 1FJU 1FJV 1FJW 1tli 2Tli 3tli 4tli 5tli 6tli 7tli 8TLI
• Descriptor: THERMOLYSIN, ZINC ION, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: metalloproteinase, organic solvent, hydrolase
• Biological source: Bacillus thermoproteolyticus
• Cellular location: Secreted: P00800
• Total number of polymer chains: 1
• Total formula weight: 34930.50

Authors

English, A.C.,Groom, C.R.,Hubbard, R.E. (deposition date: 2000-08-08, release date: 2001-04-18, Last modification date: 2024-02-07)

Primary citation

English, A.C.,Groom, C.R.,Hubbard, R.E.
Experimental and computational mapping of the binding surface of a crystalline protein.
Protein Eng., 14:47-59, 2001

PubMed Abstract: Multiple Solvent Crystal Structures (MSCS) is a crystallographic technique to identify energetically favorable positions and orientations of small organic molecules on the surface of proteins. We determined the high-resolution crystal structures of thermolysin (TLN), generated from crystals soaked in 50--70% acetone, 50--80% acetonitrile and 50 mM phenol. The structures of the protein in the aqueous-organic mixtures are essentially the same as the native enzyme and a number of solvent interaction sites were identified. The distribution of probe molecules shows clusters in the main specificity pocket of the active site and a buried subsite. Within the active site, we compared the experimentally determined solvent positions with predictions from two computational functional group mapping techniques, GRID and Multiple Copy Simultaneous Search (MCSS). The experimentally determined small molecule positions are consistent with the structures of known protein--ligand complexes of TLN.

PubMed: 11287678
DOI: 10.1093/protein/14.1.47

Experimental method

X-RAY DIFFRACTION (2.2 Å)