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2QFL

Structure of SuhB: Inositol monophosphatase and extragenic suppressor from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001072molecular_functiontranscription antitermination factor activity, RNA binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006020biological_processinositol metabolic process
A0007165biological_processsignal transduction
A0008934molecular_functioninositol monophosphate 1-phosphatase activity
A0016787molecular_functionhydrolase activity
A0031403molecular_functionlithium ion binding
A0031564biological_processtranscription antitermination
A0042134molecular_functionrRNA primary transcript binding
A0042254biological_processribosome biogenesis
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 375
ChainResidue
AGLY88
ATHR89
ALYS160
AEEE376
AHOH1041

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EEE A 376
ChainResidue
AALA188
AACT375
AHOH1007
AHOH1013
AHOH1027
AASP87
ATHR89
AGLY186
ASER187

Functional Information from PROSITE/UniProt
site_idPS00629
Number of Residues14
DetailsIMP_1 Inositol monophosphatase family signature 1. WvIDPLDGTtnFiK
ChainResidueDetails
ATRP81-LYS94

site_idPS00630
Number of Residues15
DetailsIMP_2 Inositol monophosphatase family signature 2. WDfAAGeLLVreaGG
ChainResidueDetails
ATRP211-GLY225

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU67
AARG183
AASP212

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31020314, ECO:0000269|PubMed:32871103
ChainResidueDetails
AASP84
ALEU86

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
AGLU67
ATHR89

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PDB entries from 2024-07-24

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