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3O6Z

Structure of the D152A E.coli GDP-mannose hydrolase (yffh) in complex with Mg++

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006753biological_processnucleoside phosphate metabolic process
A0016787molecular_functionhydrolase activity
A0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
A0019693biological_processribose phosphate metabolic process
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0052751molecular_functionGDP-mannose hydrolase activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0006753biological_processnucleoside phosphate metabolic process
B0016787molecular_functionhydrolase activity
B0016818molecular_functionhydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
B0019693biological_processribose phosphate metabolic process
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0052751molecular_functionGDP-mannose hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AALA85
AGLU104
AHOH311
AHOH324
AHOH417

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 201
ChainResidue
BHOH229
BHOH414
BHOH415
BGLU100
BGLU104
BGLU151
BMG202

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG B 202
ChainResidue
BALA85
BGLU104
BGLU151
BMG201
BHOH214
BHOH240
BHOH347
BHOH414

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 204
ChainResidue
BARG113

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 203
ChainResidue
BGLN4
BTHR28

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG B 205
ChainResidue
BGLU94
BVAL95
BLYS99
BHOH327
BHOH350

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS B 206
ChainResidue
BARG64
BILE81
BMET166
BGLU171

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG B 192
ChainResidue
AILE8
AARG36
BASP15
BTHR19
BHIS21
BASP43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"21638333","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O61","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21638333","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O61","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21638333","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3O6Z","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues137
DetailsDomain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues27
DetailsMotif: {"description":"Nudix box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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