3W00
Crystal structure of PcrB complexed with G1P and FsPP from bacillus subtilis subap. subtilis str. 168
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006650 | biological_process | glycerophospholipid metabolic process |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0046474 | biological_process | glycerophospholipid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120536 | molecular_function | heptaprenylglyceryl phosphate synthase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006650 | biological_process | glycerophospholipid metabolic process |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0046474 | biological_process | glycerophospholipid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0120536 | molecular_function | heptaprenylglyceryl phosphate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 600 |
| Chain | Residue |
| A | SER162 |
| A | GLY163 |
| A | GLY188 |
| A | ASN209 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FPS B 301 |
| Chain | Residue |
| B | HIS97 |
| B | LYS126 |
| B | GLU160 |
| B | 1GP302 |
| B | HOH422 |
| B | SER40 |
| B | VAL66 |
| B | ILE69 |
| B | PRO82 |
| B | TRP92 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 1GP B 302 |
| Chain | Residue |
| B | LYS12 |
| B | TYR158 |
| B | GLU160 |
| B | SER162 |
| B | GLY187 |
| B | GLY188 |
| B | GLY208 |
| B | ASN209 |
| B | FPS301 |
| B | HOH412 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00112","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23322418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3W00","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00112","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
