6H5A
Crystal structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase (PgsA1) in complex with manganese and citrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003881 | molecular_function | CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| A | 0046474 | biological_process | glycerophospholipid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003881 | molecular_function | CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| B | 0046474 | biological_process | glycerophospholipid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 301 |
| Chain | Residue |
| A | ASP68 |
| A | ASP71 |
| A | ASP89 |
| A | HOH440 |
| A | HOH445 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MN A 302 |
| Chain | Residue |
| A | ASP68 |
| A | ASP89 |
| A | ASP93 |
| A | FLC305 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 303 |
| Chain | Residue |
| A | MN304 |
| A | FLC305 |
| A | FLC306 |
| A | HOH427 |
| A | HOH464 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MN A 304 |
| Chain | Residue |
| A | MN303 |
| A | FLC305 |
| A | FLC306 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue FLC A 305 |
| Chain | Residue |
| A | ARG9 |
| A | ASP68 |
| A | ASP89 |
| A | ASP93 |
| A | ARG152 |
| A | PRO153 |
| A | MN302 |
| A | MN303 |
| A | MN304 |
| A | FLC306 |
| A | HOH403 |
| A | HOH407 |
| A | HOH427 |
| A | HOH438 |
| A | HOH440 |
| A | HOH464 |
| B | PHE222 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue FLC A 306 |
| Chain | Residue |
| A | ALA90 |
| A | SER132 |
| A | LYS135 |
| A | ARG195 |
| A | MN303 |
| A | MN304 |
| A | FLC305 |
| A | HOH405 |
| A | HOH406 |
| A | HOH420 |
| A | HOH438 |
| A | HOH441 |
| A | HOH464 |
| B | ARG137 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 307 |
| Chain | Residue |
| A | TRP106 |
| B | ILE119 |
| B | ILE123 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue OLC A 308 |
| Chain | Residue |
| A | SER8 |
| A | ARG9 |
| A | TRP62 |
| A | GLU154 |
| A | ILE157 |
| A | HOH401 |
| A | HOH449 |
| A | HOH457 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue LFA A 309 |
| Chain | Residue |
| A | ALA40 |
| A | THR47 |
| A | MET51 |
| A | LYS53 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue MN B 301 |
| Chain | Residue |
| B | GLU151 |
| B | FLC304 |
| B | HOH441 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 302 |
| Chain | Residue |
| B | ASP68 |
| B | ASP71 |
| B | ASP89 |
| B | MN303 |
| B | HOH402 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 303 |
| Chain | Residue |
| B | ASP68 |
| B | ASP89 |
| B | ASP93 |
| B | MN302 |
| B | HOH403 |
| B | HOH404 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue FLC B 304 |
| Chain | Residue |
| B | SER132 |
| B | LYS135 |
| B | GLU151 |
| B | ARG152 |
| B | ARG155 |
| B | ARG195 |
| B | MN301 |
| B | HOH419 |
| B | HOH422 |
| B | HOH441 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue OLC B 305 |
| Chain | Residue |
| B | ILE19 |
| B | GLY22 |
| B | ARG25 |
| B | VAL26 |
| B | ASP114 |
| B | PRO116 |
| B | LEU117 |
| B | SER178 |
| B | TRP182 |
| B | VAL186 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 306 |
| Chain | Residue |
| B | PRO203 |
| B | GLY204 |
| B | ARG217 |
| B | ASN219 |
| B | HOH401 |
| A | ARG14 |
| B | SER202 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue LFA B 307 |
| Chain | Residue |
| B | ILE95 |
| B | TRP106 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue 1PE B 308 |
| Chain | Residue |
| B | GLY52 |
| B | LEU54 |
| B | TRP107 |
| B | HIS111 |
| B | MET112 |
| B | SER166 |
| B | ASP167 |
| B | PRO174 |
| B | HOH414 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue 1PE B 309 |
| Chain | Residue |
| A | GLY52 |
| A | TRP107 |
| A | MET112 |
| A | SER166 |
| A | PRO174 |
| A | ALA210 |
| B | GLY79 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue LFA B 310 |
| Chain | Residue |
| B | THR47 |
Functional Information from PROSITE/UniProt
| site_id | PS00379 |
| Number of Residues | 23 |
| Details | CDP_ALCOHOL_P_TRANSF CDP-alcohol phosphatidyltransferases signature. DGamARergggtrfGavlDatcD |
| Chain | Residue | Details |
| A | ASP71-ASP93 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 262 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:31098408 |
| Chain | Residue | Details |
| A | PRO30-LEU48 | |
| B | ARG115-ALA140 | |
| B | ARG152-SER166 | |
| B | ALA176-TRP200 | |
| A | LEU54-GLU77 | |
| A | ARG83-PHE110 | |
| A | ARG115-ALA140 | |
| A | ARG152-SER166 | |
| A | ALA176-TRP200 | |
| B | PRO30-LEU48 | |
| B | LEU54-GLU77 | |
| B | ARG83-PHE110 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:31098408 |
| Chain | Residue | Details |
| A | ASP93 | |
| B | ASP93 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31098408 |
| Chain | Residue | Details |
| A | ASP31 | |
| B | ASP68 | |
| B | ASP71 | |
| B | GLY72 | |
| B | ARG76 | |
| B | THR82 | |
| B | ASP89 | |
| B | ASP93 | |
| A | ASP68 | |
| A | ASP71 | |
| A | GLY72 | |
| A | ARG76 | |
| A | THR82 | |
| A | ASP89 | |
| A | ASP93 | |
| B | ASP31 |
