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4C5F

Structure of Lytic Transglycosylase MltC from Escherichia coli at 2.3 A resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0008932molecular_functionlytic endotransglycosylase activity
A0008933molecular_functionlytic transglycosylase activity
A0009253biological_processpeptidoglycan catabolic process
A0009279cellular_componentcell outer membrane
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016829molecular_functionlyase activity
A0016998biological_processcell wall macromolecule catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034599biological_processcellular response to oxidative stress
A0051301biological_processcell division
A0071236biological_processcellular response to antibiotic
A0071555biological_processcell wall organization
B0000270biological_processpeptidoglycan metabolic process
B0008932molecular_functionlytic endotransglycosylase activity
B0008933molecular_functionlytic transglycosylase activity
B0009253biological_processpeptidoglycan catabolic process
B0009279cellular_componentcell outer membrane
B0016020cellular_componentmembrane
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016829molecular_functionlyase activity
B0016998biological_processcell wall macromolecule catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0034599biological_processcellular response to oxidative stress
B0051301biological_processcell division
B0071236biological_processcellular response to antibiotic
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00922
Number of Residues29
DetailsTRANSGLYCOSYLASE Prokaryotic transglycosylases signature. ImqtESsfnPyavSrsdalGLMqVvqhtA
ChainResidueDetails
AILE213-ALA241

227344

PDB entries from 2024-11-13

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