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2GT4

Crystal Structure of the Y103F mutant of the GDP-mannose mannosyl hydrolase in complex with GDP-mannose and MG+2

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
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 Residues3
DetailsBINDING:
ChainResidueDetails
APHE3
BPHE3
CPHE3

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00941, ECO:0000269|PubMed:15274914, ECO:0000269|PubMed:16981689
ChainResidueDetails
APHE9
BGLN123
CPHE9
CARG37
CGLY50
CGLU70
CGLN123
AARG37
AGLY50
AGLU70
AGLN123
BPHE9
BARG37
BGLY50
BGLU70

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Critical for catalysis
ChainResidueDetails
AHIS124
BHIS124
CHIS124

219140

PDB entries from 2024-05-01

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