Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2IK4

Yeast inorganic pyrophosphatase variant D117E with magnesium and phosphate

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 MG A 287
ChainResidue
AASP115
AASP120
AASP152
AHOH289
AHOH293
AHOH294

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 288
ChainResidue
AHOH292
AHOH295
AHOH296
AASP120
AHOH290
AHOH291

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG B 287
ChainResidue
BASP115
BGLU117
BASP120
BASP152
BMG288
BMG289
BPO4290
BHOH291

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 288
ChainResidue
BGLU117
BASP120
BMG287
BPO4290
BHOH292
BHOH293
BHOH294

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 289
ChainResidue
BASP147
BASP152
BMG287
BPO4290
BHOH295
BHOH296
BHOH297

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PO4 B 290
ChainResidue
BLYS56
BGLU58
BTYR93
BASP115
BGLU117
BASP120
BASP152
BLYS154
BMG287
BMG288
BMG289
BHOH294
BHOH295
BHOH296
BHOH297
BHOH376
BHOH427

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:1322842
ChainResidueDetails
AILE90
BILE90

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
APHE79
AASN116
AVAL121
ATRP153
BPHE79
BASN116
BVAL121
BTRP153

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ALEU65
BLEU65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950
ChainResidueDetails
APRO251
BPRO251

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ALEU266
BLEU266

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377
ChainResidueDetails
AVAL286
BVAL286

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
AGLY239
ATRP279
BGLY239
BTRP279

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1wgi
ChainResidueDetails
AGLU117

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1wgi
ChainResidueDetails
BGLU117

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon