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2UXS

2.7A crystal structure of inorganic pyrophosphatase (Rv3628) from Mycobacterium tuberculosis at pH 7.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004427molecular_functioninorganic diphosphate phosphatase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006796biological_processphosphate-containing compound metabolic process
A0016787molecular_functionhydrolase activity
A0044228cellular_componenthost cell surface
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004427molecular_functioninorganic diphosphate phosphatase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006796biological_processphosphate-containing compound metabolic process
B0016787molecular_functionhydrolase activity
B0044228cellular_componenthost cell surface
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004427molecular_functioninorganic diphosphate phosphatase activity
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006796biological_processphosphate-containing compound metabolic process
C0016787molecular_functionhydrolase activity
C0044228cellular_componenthost cell surface
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A1167
ChainResidue
ALYS23
AARG37
ATYR133
ALYS134

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B1167
ChainResidue
BLYS23
BARG37
BTYR133
BLYS134

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C1167
ChainResidue
CARG37
CTYR133
CLYS134
CLYS23

Functional Information from PROSITE/UniProt
site_idPS00387
Number of Residues7
DetailsPPASE Inorganic pyrophosphatase signature. DGDPLDA
ChainResidueDetails
AASP59-ALA65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:26296329
ChainResidueDetails
AASP96
BASP96
CASP96

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000305|PubMed:26296329
ChainResidueDetails
AGLU15
BASP59
BASP64
BASP91
BASP96
CGLU15
CASP59
CASP64
CASP91
CASP96
AASP59
AASP64
AASP91
AASP96
BGLU15

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:26296329
ChainResidueDetails
ATYR133
BLYS23
BARG37
BTYR49
BTYR133
CLYS23
CARG37
CTYR49
CTYR133
ALYS23
AARG37
ATYR49

219869

PDB entries from 2024-05-15

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