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1O12

Crystal structure of N-acetylglucosamine-6-phosphate deacetylase (TM0814) from Thermotoga maritima at 2.5 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0006040biological_processamino sugar metabolic process
A0006044biological_processN-acetylglucosamine metabolic process
A0006046biological_processN-acetylglucosamine catabolic process
A0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
B0006040biological_processamino sugar metabolic process
B0006044biological_processN-acetylglucosamine metabolic process
B0006046biological_processN-acetylglucosamine catabolic process
B0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 401
ChainResidue
AGLU115
AHIS176
AHIS197
AHOH408
AHOH491

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 401
ChainResidue
BHOH407
BGLU115
BHIS176
BHIS197
BHOH405

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PDB entries from 2024-07-31

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