3VZZ
Crystal structure of PcrB complexed with 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 | 6 |
Details | BINDING SITE FOR RESIDUE MG A 301 |
Chain | Residue |
A | ARG56 |
A | PHE58 |
A | HOH479 |
A | HOH480 |
A | HOH481 |
A | HOH555 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 302 |
Chain | Residue |
A | LEU59 |
A | HOH484 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE FPS B 301 |
Chain | Residue |
B | SER40 |
B | VAL66 |
B | ILE69 |
B | PRO82 |
B | TRP92 |
B | ALA100 |
B | GLU160 |
B | HOH424 |
B | HOH425 |
B | HOH535 |
B | LYS12 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 302 |
Chain | Residue |
B | ARG56 |
B | PHE58 |
B | HOH439 |
B | HOH440 |
B | HOH512 |
B | HOH533 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 303 |
Chain | Residue |
B | THR44 |
B | GLU45 |
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 |