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1WCF

1.54 A CRYSTAL STRUCTURE OF RV3628, MYCOBACTERIUM TUBERCULOSIS INORGANIC PYROPHOSPHATASE (PPASE) AT PH7.0

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 Residues5
DetailsBINDING SITE FOR RESIDUE K A 1162
ChainResidue
ALYS127
AASP128
AGLU130
ALYS133
AHOH2236

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 1163
ChainResidue
AHOH2147
AHOH2180
APRO55
AASP57
AASP89
AHOH2140

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 1164
ChainResidue
ALYS16
AGLU18
AASP29
AARG30
ATYR126
ALYS127
AHOH2277
AHOH2279

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

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1wgi
ChainResidueDetails
AASP54

224004

PDB entries from 2024-08-21

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