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8PRK

THE R78K AND D117E ACTIVE SITE VARIANTS OF SACCHAROMYCES CEREVISIAE SOLUBLE INORGANIC PYROPHOSPHATASE: STRUCTURAL STUDIES AND MECHANISTIC IMPLICATIONS

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 Residues6
DetailsBINDING SITE FOR RESIDUE MN B 2005
ChainResidue
BASP1115
BASP1120
BASP1152
BMN2008
BPO43004
BHOH4008

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 2004
ChainResidue
AASP147
AASP152
APO43002

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 2008
ChainResidue
BASP1147
BASP1152
BMN2005
BPO43004
BHOH4012

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 2006
ChainResidue
BASP1120
BPO43004
BHOH4009
BHOH4010
BHOH4011

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 2002
ChainResidue
AASP120
APO43002
AHOH4002
AHOH4003
AHOH4004

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 2001
ChainResidue
AASP115
AASP120
AASP152
APO43002
AHOH4001

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 3002
ChainResidue
ALYS56
ATYR93
AASP115
AASP117
AASP120
AASP152
ALYS154
AMN2001
AMN2002
AMN2004
AHOH4021
AHOH4262

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 B 3004
ChainResidue
BLYS1056
BTYR1093
BASP1115
BASP1117
BASP1120
BASP1152
BLYS1154
BMN2005
BMN2006
BMN2008
BHOH4012
BHOH4202

site_idMN1
Number of Residues4
DetailsMETAL 1 BINDING SITE
ChainResidue
AASP117
AASP152
AASP115
AASP120

site_idMN2
Number of Residues3
DetailsMETAL 2 BINDING SITE
ChainResidue
AASP117
ATYR93
AASP120

site_idMN4
Number of Residues2
DetailsMETAL 4 BINDING SITE
ChainResidue
AASP152
AASP147

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
BTYR1089

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
BLYS1078
BASP1115
BASP1120
BASP1152
ALYS78
AASP115
AASP120
AASP152

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATHR64
BTHR1064

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950
ChainResidueDetails
ATHR250
BTHR1250

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
BSER1265
ASER265

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377
ChainResidueDetails
ASER285
BSER1285

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS278
BLYS1238
BLYS1278
ALYS238

221051

PDB entries from 2024-06-12

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