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3OUR

Crystal structure of complex between EIIA and a novel pyruvate decarboxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0052689molecular_functioncarboxylic ester hydrolase activity
A0106435molecular_functioncarboxylesterase activity
B0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
C0016788molecular_functionhydrolase activity, acting on ester bonds
C0052689molecular_functioncarboxylic ester hydrolase activity
C0106435molecular_functioncarboxylesterase activity
D0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
E0016788molecular_functionhydrolase activity, acting on ester bonds
E0052689molecular_functioncarboxylic ester hydrolase activity
E0106435molecular_functioncarboxylesterase activity
F0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
G0016788molecular_functionhydrolase activity, acting on ester bonds
G0052689molecular_functioncarboxylic ester hydrolase activity
G0106435molecular_functioncarboxylesterase activity
H0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
Functional Information from PROSITE/UniProt
site_idPS00371
Number of Residues13
DetailsPTS_EIIA_TYPE_1_HIS PTS EIIA domains phosphorylation site signature 1. GveLFVHFGIdTV
ChainResidueDetails
BGLY85-VAL97

222926

PDB entries from 2024-07-24

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