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1IME

STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006020biological_processinositol metabolic process
A0006021biological_processinositol biosynthetic process
A0006661biological_processphosphatidylinositol biosynthetic process
A0006796biological_processphosphate-containing compound metabolic process
A0007165biological_processsignal transduction
A0008934molecular_functioninositol monophosphate 1-phosphatase activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0031403molecular_functionlithium ion binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046872molecular_functionmetal ion binding
A0052832molecular_functioninositol monophosphate 3-phosphatase activity
A0052833molecular_functioninositol monophosphate 4-phosphatase activity
A0052834molecular_functioninositol monophosphate phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006020biological_processinositol metabolic process
B0006021biological_processinositol biosynthetic process
B0006661biological_processphosphatidylinositol biosynthetic process
B0006796biological_processphosphate-containing compound metabolic process
B0007165biological_processsignal transduction
B0008934molecular_functioninositol monophosphate 1-phosphatase activity
B0016787molecular_functionhydrolase activity
B0030145molecular_functionmanganese ion binding
B0031403molecular_functionlithium ion binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046854biological_processphosphatidylinositol phosphate biosynthetic process
B0046872molecular_functionmetal ion binding
B0052832molecular_functioninositol monophosphate 3-phosphatase activity
B0052833molecular_functioninositol monophosphate 4-phosphatase activity
B0052834molecular_functioninositol monophosphate phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 278
ChainResidue
AGLU70
AASP90
AILE92
AHOH284
AHOH291

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 278
ChainResidue
BGLU70
BASP90
BILE92
BHOH286
BHOH290

site_idM1
Number of Residues8
DetailsACTIVE SITE
ChainResidue
AGLU70
AASP90
APRO91
AILE92
AASP93
AGLY94
ATHR95
AASP220

site_idM2
Number of Residues8
DetailsACTIVE SITE
ChainResidue
BASP90
BPRO91
BILE92
BASP93
BGLY94
BTHR95
BASP220
BGLU70

Functional Information from PROSITE/UniProt
site_idPS00629
Number of Residues14
DetailsIMP_1 Inositol monophosphatase family signature 1. WiIDPIDGTtnFvH
ChainResidueDetails
ATRP87-HIS100

site_idPS00630
Number of Residues15
DetailsIMP_2 Inositol monophosphatase family signature 2. WDvAGAgIIVteaGG
ChainResidueDetails
ATRP219-GLY233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8068620, ECO:0000303|PubMed:8068621
ChainResidueDetails
AGLU70
AGLU213
BGLU70
BGLU213

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621
ChainResidueDetails
AASP90
AASP93
BASP90
BASP93

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621, ECO:0000303|PubMed:1332026, ECO:0000303|PubMed:8068620
ChainResidueDetails
AILE92
BILE92

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8068620
ChainResidueDetails
AGLY194
AASP220
BGLY194
BASP220

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR168
BTHR168

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
ATHR95
AGLU70

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
BTHR95
BGLU70

site_idMCSA1
Number of Residues6
DetailsM-CSA 577
ChainResidueDetails
AGLU70metal ligand, proton acceptor, proton donor
AASP90metal ligand
AILE92metal ligand
AASP93metal ligand
ATHR95hydrogen bond acceptor
AASP220metal ligand

site_idMCSA2
Number of Residues6
DetailsM-CSA 577
ChainResidueDetails
BGLU70metal ligand, proton acceptor, proton donor
BASP90metal ligand
BILE92metal ligand
BASP93metal ligand
BTHR95hydrogen bond acceptor
BASP220metal ligand

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PDB entries from 2024-10-30

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