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4I9G

Crystal structure of glycerol phosphate phosphatase Rv1692 from Mycobacterium tuberculosis in complex with magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000121molecular_functionglycerol-1-phosphatase activity
A0000287molecular_functionmagnesium ion binding
A0006071biological_processglycerol metabolic process
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0030145molecular_functionmanganese ion binding
A0042803molecular_functionprotein homodimerization activity
A0046475biological_processglycerophospholipid catabolic process
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
B0000121molecular_functionglycerol-1-phosphatase activity
B0000287molecular_functionmagnesium ion binding
B0006071biological_processglycerol metabolic process
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0030145molecular_functionmanganese ion binding
B0042803molecular_functionprotein homodimerization activity
B0046475biological_processglycerophospholipid catabolic process
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 400
ChainResidue
AASP14
AASP16
AASP209

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 400
ChainResidue
BASP14
BASP16
BASP209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q96GD0
ChainResidueDetails
AASP14
BASP14

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q96GD0
ChainResidueDetails
AASP16
BASP16

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23801751, ECO:0007744|PDB:4I9G
ChainResidueDetails
BASP16
BASP209
AASP14
AASP16
AASP209
BASP14

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PDB entries from 2024-06-12

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