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1OBW

STRUCTURE OF INORGANIC PYROPHOSPHATASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004427molecular_functioninorganic diphosphate phosphatase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006796biological_processphosphate-containing compound metabolic process
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0050355molecular_functioninorganic triphosphate phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0004427molecular_functioninorganic diphosphate phosphatase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006796biological_processphosphate-containing compound metabolic process
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0050355molecular_functioninorganic triphosphate phosphatase activity
C0000287molecular_functionmagnesium ion binding
C0004427molecular_functioninorganic diphosphate phosphatase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006796biological_processphosphate-containing compound metabolic process
C0008270molecular_functionzinc ion binding
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
C0050355molecular_functioninorganic triphosphate phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 176
ChainResidue
AASP65
AASP70
AASP102
AHOH198
AHOH200
AHOH202

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 176
ChainResidue
CHOH200
CHOH232
CHOH232
CHOH187
CHOH187
CHOH200

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 177
ChainResidue
CASP65
CASP70
CASP102
CHOH195
CHOH218
CHOH254

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 177
ChainResidue
AHOH201
AHOH203
AHOH209
BHOH194
BHOH201
BHOH213

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 176
ChainResidue
BASP65
BASP70
BASP102
BHOH209
BHOH242
BHOH253

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 178
ChainResidue
AASP70
AHOH213
AHOH217
AHOH224
AHOH225
AHOH242

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 177
ChainResidue
BASP70
BHOH206
BHOH211
BHOH233
BHOH237
BHOH239

Functional Information from PROSITE/UniProt
site_idPS00387
Number of Residues7
DetailsPPASE Inorganic pyrophosphatase signature. DGDPVDV
ChainResidueDetails
AASP65-VAL71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00209
ChainResidueDetails
ATYR30
BGLY56
BGLY66
BVAL71
BALA103
BLYS142
CTYR30
CPHE44
CGLY56
CGLY66
CVAL71
APHE44
CALA103
CLYS142
AGLY56
AGLY66
AVAL71
AALA103
ALYS142
BTYR30
BPHE44

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PDB entries from 2024-04-24

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