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5JKI

Crystal structure of the first transmembrane PAP2 type phosphatidylglycerolphosphate phosphatase from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008610biological_processlipid biosynthetic process
A0008962molecular_functionphosphatidylglycerophosphatase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0042392molecular_functionsphingosine-1-phosphate phosphatase activity
A0044249biological_processcellular biosynthetic process
A1901137biological_processcarbohydrate derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue WO4 A 300
ChainResidue
ALYS96
AARG103
AGLU112
ASER119
AGLY120
AHIS121
AARG165
AHIS171

site_idAC2
Number of Residues2
Detailsbinding site for residue OLC A 301
ChainResidue
AARG89
AGLY86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:28168443
ChainResidueDetails
AMET1
ATHR75-GLY78
ALEU140-HIS146
AILE197-LYS203

site_idSWS_FT_FI2
Number of Residues115
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:28168443
ChainResidueDetails
ATYR2-ALA17
ASER56-LYS74
ALEU79-ILE99
AGLY120-HIS139
ALYS147-TYR167
AVAL173-LYS196

site_idSWS_FT_FI3
Number of Residues60
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:28168443
ChainResidueDetails
AILE18-SER55
AGLU100-SER119
ALEU168-PHE172

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donors => ECO:0000305|PubMed:28168443
ChainResidueDetails
AHIS121

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:28168443
ChainResidueDetails
AHIS171

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Stabilizes the active site histidine for nucleophilic attack => ECO:0000305|PubMed:28168443
ChainResidueDetails
AASP175

218853

PDB entries from 2024-04-24

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