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1E6A

Fluoride-inhibited substrate complex of Saccharomyces cerevisiae 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 Residues9
DetailsBINDING SITE FOR RESIDUE MN A2001
ChainResidue
AASP115
AASP120
AASP152
AMN2002
AMN2004
AHOH2334
APOP3001
AF4001
ANA4740

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A2002
ChainResidue
AASP120
AMN2001
AHOH2335
AHOH2336
AHOH2337
APOP3001
AF4001

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A2003
ChainResidue
AGLU58
AHOH2338
AHOH2339
AHOH2340
APOP3001
ANA4740

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A2004
ChainResidue
AASP147
AASP152
AMN2001
AHOH2341
AHOH2342
APOP3001

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE F A4001
ChainResidue
AASP115
AASP117
AASP120
AMN2001
AMN2002
AHOH2336
APOP3001
ANA4740

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA A4740
ChainResidue
AASP115
AASP117
AMN2001
AMN2003
AHOH2165
AHOH2339
APOP3001
AF4001

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MN B2005
ChainResidue
BASP1115
BASP1120
BASP1152
BMN2006
BMN2008
BHOH2294
BPOP3002
BPO43004
BF4010

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MN B2006
ChainResidue
BASP1120
BMN2005
BHOH2295
BHOH2296
BHOH2297
BPOP3002
BPO43004
BF4010

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B2007
ChainResidue
BGLU1058
BHOH2298
BHOH2299
BHOH2300
BPOP3002
BPO43003
BPO43004

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MN B2008
ChainResidue
BASP1147
BASP1152
BMN2005
BHOH2301
BHOH2302
BPOP3002
BPO43003
BPO43004

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PO4 B3004
ChainResidue
BLYS1056
BGLU1058
BTYR1093
BASP1115
BASP1117
BASP1120
BASP1152
BMN2005
BMN2006
BMN2007
BMN2008
BHOH2096
BHOH2297
BHOH2301
BHOH2302
BPOP3002
BPO43003
BF4010

site_idBC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F B4010
ChainResidue
BHOH2294
BHOH2295
BHOH2297
BPOP3002
BPO43004
BASP1115
BASP1117
BASP1120
BMN2005
BMN2006

site_idBC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE POP A3001
ChainResidue
ALYS56
AGLU58
AARG78
ATYR93
AASP115
AASP117
AASP120
AASP147
AASP152
ATYR192
ALYS193
AMN2001
AMN2002
AMN2003
AMN2004
AHOH2145
AHOH2335
AHOH2339
AHOH2340
AHOH2341
AF4001
ANA4740

site_idBC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE POP B3002
ChainResidue
BLYS1056
BGLU1058
BARG1078
BTYR1093
BASP1115
BASP1117
BASP1120
BASP1147
BASP1152
BTYR1192
BLYS1193
BMN2005
BMN2006
BMN2007
BMN2008
BHOH2096
BHOH2297
BHOH2300
BHOH2301
BHOH2303
BPO43003
BPO43004
BF4010

site_idBC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 B3003
ChainResidue
BLYS1056
BGLU1058
BARG1078
BASP1147
BTYR1192
BLYS1193
BMN2007
BMN2008
BHOH2300
BHOH2301
BHOH2303
BPOP3002
BPO43004

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
AILE90
BILE1090

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
BPHE1079
BASN1116
BVAL1121
BTRP1153
APHE79
AASN116
AVAL121
ATRP153

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ALEU65
BLEU1065

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950
ChainResidueDetails
APRO251
BPRO1251

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ALEU266
BLEU1266

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377
ChainResidueDetails
AVAL286
BVAL1286

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ATRP279
BGLY1239
BTRP1279
AGLY239

221051

PDB entries from 2024-06-12

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