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4IKO

Structure of Peptidyl- tRNA Hydrolase from Acinetobacter baumannii at 1.90 A resolution

Summary for 4IKO
Entry DOI10.2210/pdb4iko/pdb
Related2PTH
DescriptorPeptidyl-tRNA hydrolase, GLYCEROL, 1,2-ETHANEDIOL, ... (6 entities in total)
Functional Keywordspeptidyl-trna hydrolase, enzyme, molecular conformation, inhibition, hydrolase
Biological sourceAcinetobacter baumannii
Cellular locationCytoplasm (By similarity): D0C9L6
Total number of polymer chains1
Total formula weight21639.66
Authors
Yamini, S.,Kaushik, S.,Sinha, M.,Kaur, P.,Sharma, S.,Singh, T.P. (deposition date: 2012-12-27, release date: 2013-01-30, Last modification date: 2023-11-08)
Primary citationKaushik, 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
Cited by
PubMed: 23844024
DOI: 10.1371/journal.pone.0067547
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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