6L07
Crystal structure of Escherichia coli phosphatidylserine decarboxylase (PE-bound form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| C | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| C | 0008654 | biological_process | phospholipid biosynthetic process |
| D | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| D | 0008654 | biological_process | phospholipid biosynthetic process |
| E | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| E | 0008654 | biological_process | phospholipid biosynthetic process |
| F | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| F | 0008654 | biological_process | phospholipid biosynthetic process |
| G | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| G | 0008654 | biological_process | phospholipid biosynthetic process |
| H | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| H | 0008654 | biological_process | phospholipid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residues 9TL I 301 and PPI I 254 |
| Chain | Residue |
| A | TYR45 |
| A | VAL206 |
| A | PHE250 |
| I | THR255 |
| A | TYR137 |
| A | LEU138 |
| A | SER166 |
| A | VAL167 |
| A | VAL201 |
| A | ALA203 |
| A | THR204 |
| A | ILE205 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide PPI J 254 and THR J 255 |
| Chain | Residue |
| B | THR136 |
| B | TYR137 |
| B | LEU138 |
| B | VAL167 |
| B | PHE179 |
| B | LEU200 |
| B | VAL201 |
| B | PHE250 |
| J | VAL256 |
| J | PEE301 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residues 9TL J 301 and PPI J 254 |
| Chain | Residue |
| B | LEU13 |
| B | TYR45 |
| B | TYR137 |
| B | LEU138 |
| B | SER166 |
| B | VAL167 |
| B | ASN168 |
| B | ALA203 |
| B | THR204 |
| B | ILE205 |
| B | PHE250 |
| J | THR255 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide PPI K 254 and THR K 255 |
| Chain | Residue |
| C | THR135 |
| C | THR136 |
| C | TYR137 |
| C | LEU138 |
| C | VAL167 |
| C | PHE179 |
| C | VAL201 |
| C | PHE250 |
| K | VAL256 |
| K | PEE301 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residues 9TL K 301 and PPI K 254 |
| Chain | Residue |
| C | PHE41 |
| C | TYR45 |
| C | TYR137 |
| C | LEU138 |
| C | PRO140 |
| C | SER166 |
| C | VAL167 |
| C | ASN168 |
| C | ALA203 |
| C | THR204 |
| C | ILE205 |
| C | PHE250 |
| K | THR255 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide PPI L 254 and THR L 255 |
| Chain | Residue |
| E | THR136 |
| E | TYR137 |
| E | LEU138 |
| E | VAL167 |
| E | PHE179 |
| E | VAL201 |
| E | GLY202 |
| E | ALA203 |
| E | PHE250 |
| L | VAL256 |
| L | PEE301 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residues 9TL L 301 and PPI L 254 |
| Chain | Residue |
| E | TYR45 |
| E | TYR137 |
| E | LEU138 |
| E | PRO140 |
| E | SER166 |
| E | VAL167 |
| E | ASN168 |
| E | VAL201 |
| E | GLY202 |
| E | ALA203 |
| E | THR204 |
| E | ILE205 |
| E | PHE250 |
| L | THR255 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide PPI M 254 and THR M 255 |
| Chain | Residue |
| G | THR136 |
| G | TYR137 |
| G | LEU138 |
| G | VAL167 |
| G | PHE179 |
| G | VAL201 |
| G | VAL206 |
| G | PHE250 |
| M | VAL256 |
| M | PEE301 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residues 9TL M 301 and PPI M 254 |
| Chain | Residue |
| G | VAL201 |
| G | ALA203 |
| G | THR204 |
| G | ILE205 |
| G | VAL206 |
| G | PHE250 |
| M | THR255 |
| G | TYR45 |
| G | TYR137 |
| G | LEU138 |
| G | PRO140 |
| G | SER166 |
| G | VAL167 |
| G | ASN168 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide PYR N 254 and THR N 255 |
| Chain | Residue |
| D | THR136 |
| D | TYR137 |
| D | LEU138 |
| D | VAL167 |
| D | PHE179 |
| D | VAL201 |
| N | VAL256 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide PYR O 254 and THR O 255 |
| Chain | Residue |
| F | THR136 |
| F | TYR137 |
| F | LEU138 |
| F | VAL167 |
| F | PHE179 |
| F | VAL201 |
| F | ALA203 |
| O | VAL256 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide PYR P 254 and THR P 255 |
| Chain | Residue |
| H | THR136 |
| H | TYR137 |
| H | LEU138 |
| H | HIS144 |
| H | VAL167 |
| H | PHE179 |
| H | VAL201 |
| H | PHE250 |
| P | VAL256 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | ACT_SITE: Charge relay system; for autoendoproteolytic cleavage activity => ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-Rule:MF_00662 |
| Chain | Residue | Details |
| A | ASP90 | |
| A | HIS147 | |
| B | ASP90 | |
| B | HIS147 | |
| C | ASP90 | |
| C | HIS147 | |
| D | ASP90 | |
| D | HIS147 | |
| E | ASP90 | |
| E | HIS147 | |
| F | ASP90 | |
| F | HIS147 | |
| G | ASP90 | |
| G | HIS147 | |
| H | ASP90 | |
| H | HIS147 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | SITE: Cleavage (non-hydrolytic); by autocatalysis => ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:3042771 |
| Chain | Residue | Details |
| A | GLY253 | |
| B | GLY253 | |
| C | GLY253 | |
| D | GLY253 | |
| E | GLY253 | |
| F | GLY253 | |
| G | GLY253 | |
| H | GLY253 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:3042771 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 | |
| C | MET1 | |
| D | MET1 | |
| E | MET1 | |
| F | MET1 | |
| G | MET1 | |
| H | MET1 |
