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4LUG

Crystal structure of Inorganic Pyrophosphatase PPA1 from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004427molecular_functioninorganic diphosphate phosphatase activity
A0005737cellular_componentcytoplasm
A0006796biological_processphosphate-containing compound metabolic process
B0000287molecular_functionmagnesium ion binding
B0004427molecular_functioninorganic diphosphate phosphatase activity
B0005737cellular_componentcytoplasm
B0006796biological_processphosphate-containing compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
AASP98
AASP103
AASP135
AHOH433
AHOH440
AHOH459

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA B 301
ChainResidue
BHOH419
BHOH424
BHOH474
BHOH498
BASP98
BASP103
BASP135

Functional Information from PROSITE/UniProt
site_idPS00387
Number of Residues7
DetailsPPASE Inorganic pyrophosphatase signature. DNDPIDV
ChainResidueDetails
AASP98-VAL104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P00817
ChainResidueDetails
ATYR84
BTYR84

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WI55
ChainResidueDetails
ALYS62
AARG76
ATYR88
ATYR172
BLYS62
BARG76
BTYR88
BTYR172

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A7A9
ChainResidueDetails
AASP98
AASP103
AASP135
BASP98
BASP103
BASP135

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PDB entries from 2025-06-18

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