5AQE

Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase

Summary for 5AQE

• Entry DOI: 10.2210/pdb5aqe/pdb
• Descriptor: SUBTILISIN SAVINASE, (4-VINYLPHENYL)METHANESULFONIC ACID, SULFATE ION, ... (7 entities in total)
• Functional Keywords: hydrolase, protease, subtilisin, catalysis, palladium, metalloenzyme, heck reaction, cross-coupling
• Biological source: BACILLUS LENTUS
• Cellular location: Secreted: P29600
• Total number of polymer chains: 1
• Total formula weight: 27272.40

Authors

Sharma, M.,Diaz-Rodriguez, A.,Offen, W.A.,Palm-Espling, M.E.,Pordea, A.,Wormald, M.R.,Mcdonough, M.,Davies, G.J.,Davis, B.G. (deposition date: 2015-09-22, release date: 2015-10-07, Last modification date: 2024-01-10)

• Primary citation: Sharma, M.,Diaz-Rodriguez, A.,Offen, W.A.,Pordea, A.,Wormald, M.R.,Mcdonough, M.,Davies, G.J.,Davis, B.G.; Bisubstrate Localisation by a Tailored Serine Protease Allows Creation of a Heck-Ase; To be Published,

Experimental method

X-RAY DIFFRACTION (1.1 Å)