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5KDF

Inorganic pyrophosphatase from Mycobacterium tuberculosis in complex with inhibitor 6 and inorganic pyrophosphate

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
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue 6RU A 201
ChainResidue
AGLU115

site_idAC2
Number of Residues3
Detailsbinding site for residue CA A 202
ChainResidue
AGLU18
AASP29
APOP205

site_idAC3
Number of Residues4
Detailsbinding site for residue CA A 203
ChainResidue
ALYS127
AASP128
AGLU130
ALYS133

site_idAC4
Number of Residues3
Detailsbinding site for residue CA A 204
ChainResidue
AHOH302
AHOH307
AHOH301

site_idAC5
Number of Residues10
Detailsbinding site for residue POP A 205
ChainResidue
ALYS16
AARG30
AGLU85
AASP89
ATYR126
ALYS127
ACA202
AHOH301
AHOH315
AHOH321

Functional Information from PROSITE/UniProt
site_idPS00387
Number of Residues7
DetailsPPASE Inorganic pyrophosphatase signature. DGDPLDA
ChainResidueDetails
AASP52-ALA58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:26296329
ChainResidueDetails
AASP89

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:26296329
ChainResidueDetails
AGLU8
AASP52
AASP57
AASP84
AASP89

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26296329
ChainResidueDetails
ALYS16
AARG30
ATYR42
ATYR126

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PDB entries from 2024-07-17

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