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2RI1

Crystal Structure of glucosamine 6-phosphate deaminase (NagB) with GlcN6P from S. mutans

Functional Information from GO Data
ChainGOidnamespacecontents
A0004342molecular_functionglucosamine-6-phosphate deaminase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006040biological_processamino sugar metabolic process
A0006043biological_processglucosamine catabolic process
A0006044biological_processN-acetylglucosamine metabolic process
A0006046biological_processN-acetylglucosamine catabolic process
A0016787molecular_functionhydrolase activity
A0019262biological_processN-acetylneuraminate catabolic process
A0042802molecular_functionidentical protein binding
B0004342molecular_functionglucosamine-6-phosphate deaminase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0006040biological_processamino sugar metabolic process
B0006043biological_processglucosamine catabolic process
B0006044biological_processN-acetylglucosamine metabolic process
B0006046biological_processN-acetylglucosamine catabolic process
B0016787molecular_functionhydrolase activity
B0019262biological_processN-acetylneuraminate catabolic process
B0042802molecular_functionidentical protein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor; for enolization step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"For ring-opening step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton acceptor; for ring-opening step","evidences":[{"source":"HAMAP-Rule","id":"MF_01241","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-12-24

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