Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2WBK

Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004567molecular_functionbeta-mannosidase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006516biological_processglycoprotein catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004567molecular_functionbeta-mannosidase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006516biological_processglycoprotein catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
AGLU462
AGLN555

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bgl
ChainResidueDetails
BGLU462
BGLN555

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon