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3O69

Structure of the E100A 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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AALA85
AGLU104
AHOH213
AHOH297

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 6073
ChainResidue
AASP15
AASN16
BHIS188

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 210
ChainResidue
AGLU40
BARG44

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 214
ChainResidue
ATRP71

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 219
ChainResidue
ATHR2
BGLN65
BPHE66
BASP152
BHOH413

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA B 215
ChainResidue
BARG44
BHOH252

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 203
ChainResidue
BHOH236
BHOH305
BHOH307
BHOH308
BHOH405

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 202
ChainResidue
BALA85
BGLU104
BHOH199
BHOH218
BHOH315
BHOH365

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 250
ChainResidue
BHOH230
BHOH316
BHOH317
BHOH318
BHOH319
BHOH345

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 210
ChainResidue
BTRP71

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG B 192
ChainResidue
BGLU92
BPRO93
BGLU94
BLYS114
BPHE132
BHOH302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: in other chain => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O61
ChainResidueDetails
ATYR17
BLYS176
AARG67
AGLU127
AASP150
ALYS176
BTYR17
BARG67
BGLU127
BASP150

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O61
ChainResidueDetails
ALYS38
BLYS38

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:21638333, ECO:0007744|PDB:3O6Z
ChainResidueDetails
AALA85
AALA100
AGLU104
AGLU151
BALA85
BALA100
BGLU104
BGLU151

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PDB entries from 2024-07-24

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