4FOP

Crystal Structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.86 A resolution

Summary for 4FOP

• Entry DOI: 10.2210/pdb4fop/pdb
• Related: 2PTH
• Descriptor: Peptidyl-tRNA hydrolase, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: Acinetobacter baumannii
• Cellular location: Cytoplasm (By similarity): D0C9L6
• Total number of polymer chains: 1
• Total formula weight: 21635.67

Authors

Kaushik, S.,Kumar, S.,Singh, N.,Sinha, M.,Kaur, P.,Sharma, S.,Singh, T.P. (deposition date: 2012-06-21, release date: 2012-07-04, Last modification date: 2023-11-08)

• Primary citation: Kaushik, S.,Singh, N.,Yamini, S.,Singh, A.,Sinha, M.,Arora, A.,Kaur, P.,Sharma, S.,Singh, T.P.; The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii; Plos One, 8:e67547-e67547, 2013; PubMed: 23844024; DOI: 10.1371/journal.pone.0067547

Experimental method

X-RAY DIFFRACTION (1.86 Å)