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5DJF

Structure of M. tuberculosis CysQ, a PAP phosphatase - ligand-free structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0000103biological_processsulfate assimilation
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0008441molecular_function3'(2'),5'-bisphosphate nucleotidase activity
A0008934molecular_functioninositol monophosphate 1-phosphatase activity
A0016787molecular_functionhydrolase activity
A0030145molecular_functionmanganese ion binding
A0042132molecular_functionfructose 1,6-bisphosphate 1-phosphatase activity
A0046872molecular_functionmetal ion binding
A0050427biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process
A0050897molecular_functioncobalt ion binding
A0052832molecular_functioninositol monophosphate 3-phosphatase activity
A0052833molecular_functioninositol monophosphate 4-phosphatase activity
A0052834molecular_functioninositol monophosphate phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 301
ChainResidue
AASP50
AGLU73
AASP91
ALEU93
AHOH556

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 302
ChainResidue
AASP85
AHOH439
AASP25
AGLN32
ALEU56
ASER84

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 303
ChainResidue
APRO166
AASP196
ATYR198
AHOH413
AHOH417

Functional Information from PROSITE/UniProt
site_idPS00629
Number of Residues14
DetailsIMP_1 Inositol monophosphatase family signature 1. WiIDPLDGTreFsT
ChainResidueDetails
ATRP88-THR101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP91
ALEU93
AASP94
AASP212
AGLU73

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PDB entries from 2024-06-12

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