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8TMS

Crystal structure of bacterial pectin methylesterase PmeC2 from rumen Butyrivibrio

Functional Information from GO Data
ChainGOidnamespacecontents
A0009279cellular_componentcell outer membrane
A0016787molecular_functionhydrolase activity
A0030599molecular_functionpectinesterase activity
A0042545biological_processcell wall modification
A0045490biological_processpectin catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
B0009279cellular_componentcell outer membrane
B0016787molecular_functionhydrolase activity
B0030599molecular_functionpectinesterase activity
B0042545biological_processcell wall modification
B0045490biological_processpectin catabolic process
B0052689molecular_functioncarboxylic ester hydrolase activity
C0009279cellular_componentcell outer membrane
C0016787molecular_functionhydrolase activity
C0030599molecular_functionpectinesterase activity
C0042545biological_processcell wall modification
C0045490biological_processpectin catabolic process
C0052689molecular_functioncarboxylic ester hydrolase activity
D0009279cellular_componentcell outer membrane
D0016787molecular_functionhydrolase activity
D0030599molecular_functionpectinesterase activity
D0042545biological_processcell wall modification
D0045490biological_processpectin catabolic process
D0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00503
Number of Residues10
DetailsPECTINESTERASE_2 Pectinesterase signature 2. IeGDVDFIFG
ChainResidueDetails
AILE157-GLY166

224201

PDB entries from 2024-08-28

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