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5DJG

Structure of M. tuberculosis CysQ, a PAP phosphatase with PAP, Mg, and Li bound

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
A0052834molecular_functioninositol monophosphate phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MG A 301
ChainResidue
AGLU73
AASP91
ALEU93
ALI302
AA3P303
AHOH457
AHOH491

site_idAC2
Number of Residues5
Detailsbinding site for residue LI A 302
ChainResidue
AASP212
AMG301
AA3P303
AASP91
AASP94

site_idAC3
Number of Residues30
Detailsbinding site for residue A3P A 303
ChainResidue
AHIS-16
AGLU73
AASP91
ALEU93
AASP94
AGLY95
ATHR96
ASER162
AARG165
AGLY185
ASER186
AALA187
ALYS190
AHIS204
AGLY206
AGLY207
AGLN208
AASP212
AMG301
ALI302
AHOH424
AHOH445
AHOH449
AHOH457
AHOH473
AHOH479
AHOH480
AHOH481
AHOH501
AHOH562

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
AGLU73
AASP91
ALEU93
AASP94
AASP212

237992

PDB entries from 2025-06-25

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