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1AWB

HUMAN MYO-INOSITOL MONOPHOSPHATASE IN COMPLEX WITH D-INOSITOL-1-PHOSPHATE AND CALCIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004346molecular_functionglucose-6-phosphatase activity
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
A0008877molecular_functionglucose-1-phosphatase activity
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
A0047954molecular_functionglycerol-2-phosphatase activity
A0052832molecular_functioninositol monophosphate 3-phosphatase activity
A0052833molecular_functioninositol monophosphate 4-phosphatase activity
A0052834molecular_functioninositol monophosphate phosphatase activity
A0103026molecular_functionfructose-1-phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0004346molecular_functionglucose-6-phosphatase activity
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
B0008877molecular_functionglucose-1-phosphatase activity
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
B0047954molecular_functionglycerol-2-phosphatase activity
B0052832molecular_functioninositol monophosphate 3-phosphatase activity
B0052833molecular_functioninositol monophosphate 4-phosphatase activity
B0052834molecular_functioninositol monophosphate phosphatase activity
B0103026molecular_functionfructose-1-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1
ChainResidue
AGLU70
AASP90
AILE92
AIPD281
AHOH321
AHOH341

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 278
ChainResidue
AASP90
AASP93
AASP220
AIPD281
AHOH326

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 279
ChainResidue
AGLU70
AIPD281
AHOH291
AHOH341
AHOH403
AHOH416

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 278
ChainResidue
BIPD1
BGLU70
BASP90
BILE92
BCA279
BHOH308
BHOH321

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 279
ChainResidue
BIPD1
BASP90
BASP93
BASP220
BCA278

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 280
ChainResidue
BIPD1
BGLU70
BHOH308
BHOH375
BHOH399

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 281
ChainResidue
AHOH292
AHOH359
BGLY189
BILE190
BARG191

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 280
ChainResidue
AHIS188
AARG191
BHOH330

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE IPD B 1
ChainResidue
BGLU70
BASP90
BILE92
BASP93
BGLY94
BTHR95
BGLU162
BGLY194
BTHR195
BALA196
BGLU213
BILE216
BASP220
BCA278
BCA279
BCA280
BHOH288
BHOH308
BHOH324
BHOH371

site_idBC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE IPD A 281
ChainResidue
ACA1
AGLU70
AASP90
AILE92
AASP93
AGLY94
ATHR95
AGLU162
AGLY194
ATHR195
AALA196
AGLU213
AILE216
AASP220
ACA278
ACA279
AHOH310
AHOH330
AHOH340
AHOH341
AHOH401
AHOH403

site_idCA1
Number of Residues3
DetailsCALCIUM BINDING SITE.
ChainResidue
AGLU70
AASP90
AILE92

site_idCA2
Number of Residues3
DetailsCALCIUM BINDING SITE.
ChainResidue
AASP90
AASP93
AASP220

site_idCA3
Number of Residues1
DetailsCALCIUM BINDING SITE.
ChainResidue
AGLU70

site_idCA4
Number of Residues3
DetailsCALCIUM BINDING SITE.
ChainResidue
BILE92
BGLU70
BASP90

site_idCA5
Number of Residues3
DetailsCALCIUM BINDING SITE.
ChainResidue
BASP90
BASP93
BASP220

site_idCA6
Number of Residues1
DetailsCALCIUM BINDING SITE.
ChainResidue
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 Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23027737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23027737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1332026","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

238895

PDB entries from 2025-07-16

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