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2GT2

Structure of the E. coli GDP-mannose mannosyl hydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008727molecular_functionGDP-mannose mannosyl hydrolase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0047917molecular_functionGDP-glucosidase activity
B0000287molecular_functionmagnesium ion binding
B0008727molecular_functionGDP-mannose mannosyl hydrolase activity
B0009103biological_processlipopolysaccharide biosynthetic process
B0016787molecular_functionhydrolase activity
B0030145molecular_functionmanganese ion binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0047917molecular_functionGDP-glucosidase activity
C0000287molecular_functionmagnesium ion binding
C0008727molecular_functionGDP-mannose mannosyl hydrolase activity
C0009103biological_processlipopolysaccharide biosynthetic process
C0016787molecular_functionhydrolase activity
C0030145molecular_functionmanganese ion binding
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0047917molecular_functionGDP-glucosidase activity
D0000287molecular_functionmagnesium ion binding
D0008727molecular_functionGDP-mannose mannosyl hydrolase activity
D0009103biological_processlipopolysaccharide biosynthetic process
D0016787molecular_functionhydrolase activity
D0030145molecular_functionmanganese ion binding
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
D0047917molecular_functionGDP-glucosidase activity
Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GrvqkdEtleaAFeRLTmAElG
ChainResidueDetails
AGLY51-GLY72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsMotif: {"description":"Nudix box"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00941","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15274914","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16981689","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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