4NAE
PcrB from Geobacillus kaustophilus, with bound G1P
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0002094 | molecular_function | polyprenyltransferase activity |
| A | 0004659 | molecular_function | prenyltransferase activity |
| 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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0002094 | molecular_function | polyprenyltransferase activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1GP A 301 |
| Chain | Residue |
| A | LYS12 |
| A | HOH445 |
| A | HOH457 |
| A | HOH489 |
| A | TYR159 |
| A | GLU161 |
| A | GLY164 |
| A | GLY187 |
| A | GLY188 |
| A | GLY189 |
| A | GLY209 |
| A | ASN210 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PE4 A 302 |
| Chain | Residue |
| A | VAL66 |
| A | THR67 |
| A | PRO82 |
| A | TRP92 |
| A | ARG96 |
| A | ALA100 |
| A | VAL101 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 1GP B 301 |
| Chain | Residue |
| B | LYS12 |
| B | TYR159 |
| B | GLU161 |
| B | GLY164 |
| B | GLY187 |
| B | GLY188 |
| B | GLY189 |
| B | VAL207 |
| B | GLY209 |
| B | ASN210 |
| B | HOH461 |
| B | HOH462 |
| B | HOH463 |
| B | HOH468 |
| B | HOH473 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PE4 B 302 |
| Chain | Residue |
| B | VAL66 |
| B | THR67 |
| B | PRO82 |
| B | ARG96 |
| B | ALA100 |
| B | MET108 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4NAE |
| Chain | Residue | Details |
| B | LYS12 | |
| B | TYR159 | |
| B | GLY189 | |
| B | GLY209 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00112 |
| Chain | Residue | Details |
| B | ASP14 | |
| B | THR40 |
