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1RYA

Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1001
ChainResidue
AGLY50
AGLU70
AGLN123
AGDP770
AHOH1002

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1002
ChainResidue
BHOH1004
BGLY50
BGLU70
BGLN123
BGDP771

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1003
ChainResidue
BSER28
BGLU114

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GDP A 770
ChainResidue
APHE3
ALEU4
APHE9
AARG37
AASN39
AGLY50
AGLY51
AARG52
AGLU70
APHE94
ATYR103
AGLN123
ATRS870
AMG1001
AHOH1002
AHOH1003
AHOH1010
AHOH1018
AHOH1040
AHOH1075
AHOH1078
AHOH1102
AHOH1103
AHOH1132
AHOH1153

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GDP B 771
ChainResidue
BPHE3
BLEU4
BPHE9
BARG37
BASN39
BGLY50
BGLY51
BARG52
BGLU70
BPHE94
BTYR103
BGLN123
BTRS871
BMG1002
BHOH1004
BHOH1006
BHOH1007
BHOH1012
BHOH1034
BHOH1067
BHOH1082
BHOH1135
BHOH1164
BHOH1179
BHOH1189

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS A 870
ChainResidue
ASER20
AASP22
AARG37
APHE47
AHIS88
ATYR90
ATYR103
AGDP770
AHOH1005

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS B 871
ChainResidue
BSER20
BASP22
BARG37
BPHE47
BHIS88
BTYR90
BTYR103
BGDP771
BHOH1009

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 Residues280
DetailsDomain: {"description":"Nudix hydrolase","evidences":[{"source":"HAMAP-Rule","id":"MF_00941","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues42
DetailsMotif: {"description":"Nudix box"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
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

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Critical for catalysis"}
ChainResidueDetails

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PDB entries from 2025-10-15

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