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1M38

Structure of Inorganic Pyrophosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004427molecular_functioninorganic diphosphate phosphatase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006796biological_processphosphate-containing compound metabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004427molecular_functioninorganic diphosphate phosphatase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006796biological_processphosphate-containing compound metabolic process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
AASP115
AASP120
AASP152
ACO402
APO43301
AHOH3667
AHOH3668
AHOH3670

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
ACO401
APO43301
AHOH3324
AHOH3667
AHOH3669
AHOH3671
AHOH3672
AASP120

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 403
ChainResidue
ALYS56
AGLU58
APO43301
AHOH3464

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 404
ChainResidue
AASP147
AASP152
APO43301
AHOH3364
AHOH3386
AHOH3565
AHOH3668

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO B 401
ChainResidue
BASP115
BASP120
BASP152
BHOH3545
BHOH3788
BHOH3789

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO B 402
ChainResidue
BASP120
BHOH3542
BHOH3545
BHOH3790
BHOH3791
BHOH3792
BHOH3793

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 3501
ChainResidue
ALYS74
BLYS56
BARG78
BASP147
BTYR192
BLYS193
BHOH3642
BHOH3653
BHOH3766
BHOH3781

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PO4 A 3301
ChainResidue
ALYS56
AGLU58
ATYR93
AASP115
AASP117
AASP120
AASP152
ACO401
ACO402
ACO403
ACO404
AHOH3364
AHOH3464
AHOH3565
AHOH3667
AHOH3668
AHOH3669
AHOH3672

Functional Information from PROSITE/UniProt
site_idPS00387
Number of Residues7
DetailsPPASE Inorganic pyrophosphatase signature. DNDPIDV
ChainResidueDetails
AASP115-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:1322842
ChainResidueDetails
ATYR89
BTYR89

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AARG78
AASP115
AASP120
AASP152
BARG78
BASP115
BASP120
BASP152

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATHR64
BTHR64

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950
ChainResidueDetails
ATHR250
BTHR250

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER265
BSER265

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377
ChainResidueDetails
ASER285
BSER285

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS238
ALYS278
BLYS238
BLYS278

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1wgi
ChainResidueDetails
AASP117

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1wgi
ChainResidueDetails
BASP117

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PDB entries from 2024-07-31

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