3VZY
Crystal structure of PcrB complexed with G1P 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 | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 701 |
| Chain | Residue |
| A | ARG56 |
| A | PHE58 |
| A | MG706 |
| A | HOH830 |
| A | HOH831 |
| A | HOH832 |
| A | HOH973 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 702 |
| Chain | Residue |
| A | HOH816 |
| A | HOH817 |
| A | HOH966 |
| A | HOH1012 |
| A | HOH1089 |
| A | ASP203 |
| A | MG705 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 703 |
| Chain | Residue |
| A | GLY39 |
| A | HOH870 |
| A | HOH972 |
| A | HOH978 |
| A | HOH1043 |
| A | HOH1078 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 704 |
| Chain | Residue |
| A | HOH941 |
| A | HOH974 |
| A | HOH975 |
| A | HOH1018 |
| A | HOH1042 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 705 |
| Chain | Residue |
| A | THR5 |
| A | MG702 |
| A | HOH816 |
| A | HOH818 |
| A | HOH819 |
| A | HOH966 |
| A | HOH1030 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 706 |
| Chain | Residue |
| A | MG701 |
| A | HOH829 |
| A | HOH830 |
| A | HOH832 |
| A | HOH833 |
| A | HOH973 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 707 |
| Chain | Residue |
| A | LEU59 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 708 |
| Chain | Residue |
| A | TYR2 |
| A | TRP7 |
| A | HOH823 |
| A | HOH1076 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 709 |
| Chain | Residue |
| A | GLY188 |
| A | HOH855 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 710 |
| Chain | Residue |
| A | LEU19 |
| A | LYS54 |
| A | HOH882 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1GP B 301 |
| Chain | Residue |
| B | LYS12 |
| B | TYR158 |
| B | GLU160 |
| B | SER162 |
| B | GLY163 |
| B | GLY186 |
| B | GLY188 |
| B | GLY208 |
| B | ASN209 |
| B | HOH422 |
| B | HOH423 |
| B | HOH589 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ARG56 |
| B | PHE58 |
| B | HOH466 |
| B | HOH467 |
| B | HOH501 |
| B | HOH502 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 303 |
| Chain | Residue |
| B | THR5 |
| B | MG304 |
| B | HOH434 |
| B | HOH436 |
| B | HOH438 |
| B | HOH505 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 304 |
| Chain | Residue |
| B | ASP203 |
| B | MG303 |
| B | HOH434 |
| B | HOH504 |
| B | HOH505 |
| B | HOH506 |
| B | HOH565 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 305 |
| Chain | Residue |
| A | GLU70 |
| A | HOH951 |
| A | HOH952 |
| B | GLU45 |
| B | ASP46 |
| B | HOH486 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 306 |
| Chain | Residue |
| B | GLU45 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:23322418, ECO:0007744|PDB:3VZY, ECO:0007744|PDB:3W00 |
| Chain | Residue | Details |
| A | LYS12 | |
| A | TYR158 | |
| A | GLY188 | |
| A | GLY208 | |
| B | LYS12 | |
| B | TYR158 | |
| B | GLY188 | |
| B | GLY208 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00112 |
| Chain | Residue | Details |
| A | ASP14 | |
| A | SER40 | |
| B | ASP14 | |
| B | SER40 |
