6PMD
Structure of ClpP from Staphylococcus aureus in complex with Acyldepsipeptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004176 | molecular_function | ATP-dependent peptidase activity |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006508 | biological_process | proteolysis |
| A | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0009368 | cellular_component | endopeptidase Clp complex |
| A | 0051117 | molecular_function | ATPase binding |
| B | 0004176 | molecular_function | ATP-dependent peptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0009368 | cellular_component | endopeptidase Clp complex |
| B | 0051117 | molecular_function | ATPase binding |
| C | 0004176 | molecular_function | ATP-dependent peptidase activity |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006508 | biological_process | proteolysis |
| C | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0009368 | cellular_component | endopeptidase Clp complex |
| C | 0051117 | molecular_function | ATPase binding |
| D | 0004176 | molecular_function | ATP-dependent peptidase activity |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006508 | biological_process | proteolysis |
| D | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0009368 | cellular_component | endopeptidase Clp complex |
| D | 0051117 | molecular_function | ATPase binding |
| E | 0004176 | molecular_function | ATP-dependent peptidase activity |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006508 | biological_process | proteolysis |
| E | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| E | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0009368 | cellular_component | endopeptidase Clp complex |
| E | 0051117 | molecular_function | ATPase binding |
| F | 0004176 | molecular_function | ATP-dependent peptidase activity |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006508 | biological_process | proteolysis |
| F | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| F | 0008236 | molecular_function | serine-type peptidase activity |
| F | 0009368 | cellular_component | endopeptidase Clp complex |
| F | 0051117 | molecular_function | ATPase binding |
| G | 0004176 | molecular_function | ATP-dependent peptidase activity |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006508 | biological_process | proteolysis |
| G | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| G | 0008236 | molecular_function | serine-type peptidase activity |
| G | 0009368 | cellular_component | endopeptidase Clp complex |
| G | 0051117 | molecular_function | ATPase binding |
| I | 0004176 | molecular_function | ATP-dependent peptidase activity |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006508 | biological_process | proteolysis |
| I | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| I | 0008236 | molecular_function | serine-type peptidase activity |
| I | 0009368 | cellular_component | endopeptidase Clp complex |
| I | 0051117 | molecular_function | ATPase binding |
| K | 0004176 | molecular_function | ATP-dependent peptidase activity |
| K | 0004252 | molecular_function | serine-type endopeptidase activity |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0006508 | biological_process | proteolysis |
| K | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| K | 0008236 | molecular_function | serine-type peptidase activity |
| K | 0009368 | cellular_component | endopeptidase Clp complex |
| K | 0051117 | molecular_function | ATPase binding |
| L | 0004176 | molecular_function | ATP-dependent peptidase activity |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0006508 | biological_process | proteolysis |
| L | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| L | 0008236 | molecular_function | serine-type peptidase activity |
| L | 0009368 | cellular_component | endopeptidase Clp complex |
| L | 0051117 | molecular_function | ATPase binding |
| M | 0004176 | molecular_function | ATP-dependent peptidase activity |
| M | 0004252 | molecular_function | serine-type endopeptidase activity |
| M | 0005737 | cellular_component | cytoplasm |
| M | 0006508 | biological_process | proteolysis |
| M | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| M | 0008236 | molecular_function | serine-type peptidase activity |
| M | 0009368 | cellular_component | endopeptidase Clp complex |
| M | 0051117 | molecular_function | ATPase binding |
| N | 0004176 | molecular_function | ATP-dependent peptidase activity |
| N | 0004252 | molecular_function | serine-type endopeptidase activity |
| N | 0005737 | cellular_component | cytoplasm |
| N | 0006508 | biological_process | proteolysis |
| N | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| N | 0008236 | molecular_function | serine-type peptidase activity |
| N | 0009368 | cellular_component | endopeptidase Clp complex |
| N | 0051117 | molecular_function | ATPase binding |
| S | 0004176 | molecular_function | ATP-dependent peptidase activity |
| S | 0004252 | molecular_function | serine-type endopeptidase activity |
| S | 0005737 | cellular_component | cytoplasm |
| S | 0006508 | biological_process | proteolysis |
| S | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| S | 0008236 | molecular_function | serine-type peptidase activity |
| S | 0009368 | cellular_component | endopeptidase Clp complex |
| S | 0051117 | molecular_function | ATPase binding |
| T | 0004176 | molecular_function | ATP-dependent peptidase activity |
| T | 0004252 | molecular_function | serine-type endopeptidase activity |
| T | 0005737 | cellular_component | cytoplasm |
| T | 0006508 | biological_process | proteolysis |
| T | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| T | 0008236 | molecular_function | serine-type peptidase activity |
| T | 0009368 | cellular_component | endopeptidase Clp complex |
| T | 0051117 | molecular_function | ATPase binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 400 |
| Chain | Residue |
| A | SER98 |
| A | SER101 |
| A | ILE122 |
| A | HIS123 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 400 |
| Chain | Residue |
| B | SER98 |
| B | SER101 |
| B | ILE122 |
| B | HIS123 |
| B | LEU150 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MPD C 400 |
| Chain | Residue |
| C | VAL71 |
| C | SER98 |
| C | SER101 |
| C | ILE122 |
| C | HIS123 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MPD D 400 |
| Chain | Residue |
| D | SER98 |
| D | SER101 |
| D | ILE122 |
| D | HIS123 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MPD E 400 |
| Chain | Residue |
| E | SER98 |
| E | MET99 |
| E | SER101 |
| E | PHE102 |
| E | ILE122 |
| E | HIS123 |
| E | LEU150 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MPD F 400 |
| Chain | Residue |
| F | SER98 |
| F | SER101 |
| F | ILE122 |
| F | HIS123 |
| F | LEU150 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MPD G 400 |
| Chain | Residue |
| G | SER98 |
| G | SER101 |
| G | PHE102 |
| G | ILE122 |
| G | HIS123 |
| G | LEU150 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue MPD I 400 |
| Chain | Residue |
| I | SER98 |
| I | SER101 |
| I | ILE122 |
| I | HIS123 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MPD K 400 |
| Chain | Residue |
| K | SER98 |
| K | SER101 |
| K | ILE122 |
| K | HIS123 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue MPD L 400 |
| Chain | Residue |
| L | SER98 |
| L | SER101 |
| L | ILE122 |
| L | HIS123 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MPD M 400 |
| Chain | Residue |
| M | SER98 |
| M | MET99 |
| M | SER101 |
| M | ILE122 |
| M | HIS123 |
| M | LEU154 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MPD N 400 |
| Chain | Residue |
| N | SER98 |
| N | SER101 |
| N | ILE122 |
| N | HIS123 |
| N | LEU150 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MPD S 400 |
| Chain | Residue |
| S | SER98 |
| S | MET99 |
| S | SER101 |
| S | ILE122 |
| S | HIS123 |
| S | LEU150 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MPD T 400 |
| Chain | Residue |
| T | SER98 |
| T | SER101 |
| T | ILE122 |
| T | HIS123 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for Ligand residues MP8 H 7 through PRO H 4 bound to SER H 3 |
| Chain | Residue |
| A | ASP27 |
| A | TYR61 |
| A | TYR63 |
| A | GLN89 |
| H | SHV1 |
| H | WFP2 |
| H | SER3 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for Ligand residues MP8 J 7 through PRO J 4 bound to SER J 3 |
| Chain | Residue |
| B | ASP27 |
| B | TYR61 |
| B | TYR63 |
| B | GLN89 |
| B | ILE91 |
| B | PHE113 |
| J | WFP2 |
| J | SER3 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for Ligand residues MP8 O 7 through PRO O 4 bound to SER O 3 |
| Chain | Residue |
| C | ASP27 |
| C | TYR61 |
| C | TYR63 |
| C | GLN89 |
| C | ILE91 |
| O | SHV1 |
| O | WFP2 |
| O | SER3 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for Ligand residues MP8 P 7 through PRO P 4 bound to SER P 3 |
| Chain | Residue |
| P | SER3 |
| D | ASP27 |
| D | TYR61 |
| D | TYR63 |
| D | GLN89 |
| D | ILE91 |
| P | SHV1 |
| P | WFP2 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for Ligand residues MP8 Q 7 through PRO Q 4 bound to SER Q 3 |
| Chain | Residue |
| E | ASP27 |
| E | TYR61 |
| E | TYR63 |
| E | GLN89 |
| E | ILE91 |
| Q | WFP2 |
| Q | SER3 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for Ligand residues MP8 R 7 through PRO R 4 bound to SER R 3 |
| Chain | Residue |
| F | ASP27 |
| F | TYR61 |
| F | TYR63 |
| F | GLN89 |
| F | ILE91 |
| R | WFP2 |
| R | SER3 |
| site_id | AE3 |
| Number of Residues | 8 |
| Details | binding site for Ligand residues MP8 U 7 through PRO U 4 bound to SER U 3 |
| Chain | Residue |
| K | ASP27 |
| K | TYR61 |
| K | TYR63 |
| K | GLN89 |
| K | PHE113 |
| U | SHV1 |
| U | WFP2 |
| U | SER3 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for Ligand residues MP8 V 7 through PRO V 4 bound to SER V 3 |
| Chain | Residue |
| L | ASP27 |
| L | TYR61 |
| L | TYR63 |
| L | GLN89 |
| V | SHV1 |
| V | WFP2 |
| V | SER3 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for Ligand residues MP8 X 7 through PRO X 4 bound to SER X 3 |
| Chain | Residue |
| M | ASP27 |
| M | TYR61 |
| M | TYR63 |
| M | GLN89 |
| M | ILE91 |
| X | SHV1 |
| X | WFP2 |
| X | SER3 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for Ligand residues MP8 Y 7 through PRO Y 4 bound to SER Y 3 |
| Chain | Residue |
| S | ASP27 |
| S | TYR61 |
| S | TYR63 |
| S | GLN89 |
| S | ILE91 |
| S | PHE113 |
| Y | WFP2 |
| Y | SER3 |
| site_id | AE7 |
| Number of Residues | 7 |
| Details | binding site for Ligand residues MP8 Z 7 through PRO Z 4 bound to SER Z 3 |
| Chain | Residue |
| T | ASP27 |
| T | TYR61 |
| T | TYR63 |
| T | GLN89 |
| T | ILE91 |
| Z | WFP2 |
| Z | SER3 |
| site_id | AE8 |
| Number of Residues | 15 |
| Details | binding site for residues SHV H 1 and WFP H 2 |
| Chain | Residue |
| A | ARG23 |
| A | ASP27 |
| A | ILE29 |
| A | TYR63 |
| A | MET190 |
| B | VAL45 |
| B | LEU49 |
| B | ALA53 |
| B | THR80 |
| B | HIS83 |
| H | SER3 |
| H | PRO4 |
| H | YCP5 |
| H | ALA6 |
| H | MP87 |
| site_id | AE9 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide WFP H 2 and SER H 3 |
| Chain | Residue |
| A | TYR63 |
| A | MET190 |
| B | VAL45 |
| B | LEU49 |
| B | THR80 |
| B | HIS83 |
| H | SHV1 |
| H | PRO4 |
| H | YCP5 |
| H | ALA6 |
| H | MP87 |
| site_id | AF1 |
| Number of Residues | 13 |
| Details | binding site for residues SHV J 1 and WFP J 2 |
| Chain | Residue |
| B | ARG23 |
| B | ASP27 |
| B | ILE29 |
| B | TYR63 |
| B | ILE93 |
| C | LEU49 |
| C | GLN52 |
| C | ALA53 |
| C | THR80 |
| C | HIS83 |
| C | HOH523 |
| J | SER3 |
| J | ALA6 |
| site_id | AF2 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide WFP J 2 and SER J 3 |
| Chain | Residue |
| B | TYR63 |
| B | ILE93 |
| C | LEU49 |
| C | THR80 |
| C | HIS83 |
| C | HOH524 |
| J | SHV1 |
| J | PRO4 |
| J | ALA6 |
| J | MP87 |
| site_id | AF3 |
| Number of Residues | 15 |
| Details | binding site for residues SHV O 1 and WFP O 2 |
| Chain | Residue |
| C | ARG23 |
| C | ASP27 |
| C | ILE29 |
| C | TYR63 |
| C | ILE91 |
| D | LEU49 |
| D | GLN52 |
| D | ALA53 |
| D | THR80 |
| D | HIS83 |
| D | HOH514 |
| O | SER3 |
| O | PRO4 |
| O | ALA6 |
| O | MP87 |
| site_id | AF4 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide WFP O 2 and SER O 3 |
| Chain | Residue |
| C | TYR63 |
| C | ILE91 |
| D | LEU49 |
| D | THR80 |
| D | HIS83 |
| O | SHV1 |
| O | PRO4 |
| O | ALA6 |
| O | MP87 |
| site_id | AF5 |
| Number of Residues | 17 |
| Details | binding site for residues SHV P 1 and WFP P 2 |
| Chain | Residue |
| D | ARG23 |
| D | LEU24 |
| D | ASP27 |
| D | ILE29 |
| D | TYR63 |
| D | ILE93 |
| D | LEU115 |
| E | VAL45 |
| E | LEU49 |
| E | GLN52 |
| E | ALA53 |
| E | THR80 |
| E | HIS83 |
| E | HOH511 |
| P | SER3 |
| P | ALA6 |
| P | MP87 |
| site_id | AF6 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide WFP P 2 and SER P 3 |
| Chain | Residue |
| D | TYR63 |
| D | ILE93 |
| D | LEU115 |
| E | VAL45 |
| E | LEU49 |
| E | THR80 |
| E | HIS83 |
| P | SHV1 |
| P | PRO4 |
| P | ALA6 |
| P | MP87 |
| site_id | AF7 |
| Number of Residues | 16 |
| Details | binding site for residues SHV Q 1 and WFP Q 2 |
| Chain | Residue |
| E | ARG23 |
| E | ASP27 |
| E | ILE29 |
| E | TYR63 |
| E | LEU115 |
| F | VAL45 |
| F | LEU49 |
| F | GLN52 |
| F | ALA53 |
| F | THR80 |
| F | HIS83 |
| Q | SER3 |
| Q | PRO4 |
| Q | YCP5 |
| Q | ALA6 |
| Q | HOH101 |
| site_id | AF8 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide WFP Q 2 and SER Q 3 |
| Chain | Residue |
| E | TYR63 |
| E | LEU115 |
| F | VAL45 |
| F | LEU49 |
| F | THR80 |
| F | HIS83 |
| Q | SHV1 |
| Q | PRO4 |
| Q | YCP5 |
| Q | ALA6 |
| Q | MP87 |
| site_id | AF9 |
| Number of Residues | 14 |
| Details | binding site for residues SHV R 1 and WFP R 2 |
| Chain | Residue |
| F | ARG23 |
| F | ASP27 |
| F | ILE29 |
| F | TYR63 |
| F | ILE93 |
| G | LEU49 |
| G | GLN52 |
| G | THR80 |
| G | HIS83 |
| R | SER3 |
| R | PRO4 |
| R | YCP5 |
| R | ALA6 |
| R | HOH101 |
| site_id | AG1 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide WFP R 2 and SER R 3 |
| Chain | Residue |
| F | TYR63 |
| F | ILE93 |
| G | LEU49 |
| G | THR80 |
| G | HIS83 |
| R | SHV1 |
| R | PRO4 |
| R | YCP5 |
| R | ALA6 |
| R | MP87 |
| site_id | AG2 |
| Number of Residues | 13 |
| Details | binding site for residues SHV U 1 and WFP U 2 |
| Chain | Residue |
| K | ASP27 |
| K | ILE29 |
| K | TYR63 |
| K | ILE93 |
| L | GLN52 |
| L | ALA53 |
| L | THR80 |
| L | HIS83 |
| U | SER3 |
| U | PRO4 |
| U | YCP5 |
| U | ALA6 |
| U | MP87 |
| site_id | AG3 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide WFP U 2 and SER U 3 |
| Chain | Residue |
| K | TYR63 |
| K | ILE93 |
| L | THR80 |
| L | HIS83 |
| U | SHV1 |
| U | PRO4 |
| U | YCP5 |
| U | ALA6 |
| U | MP87 |
| site_id | AG4 |
| Number of Residues | 14 |
| Details | binding site for residues SHV V 1 and WFP V 2 |
| Chain | Residue |
| L | ARG23 |
| L | LEU24 |
| L | ASP27 |
| L | ILE29 |
| L | TYR63 |
| M | LEU49 |
| M | GLN52 |
| M | THR80 |
| M | HIS83 |
| M | HOH503 |
| V | SER3 |
| V | PRO4 |
| V | ALA6 |
| V | MP87 |
| site_id | AG5 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide WFP V 2 and SER V 3 |
| Chain | Residue |
| L | TYR63 |
| M | LEU49 |
| M | THR80 |
| M | HIS83 |
| V | SHV1 |
| V | PRO4 |
| V | ALA6 |
| V | MP87 |
| site_id | AG6 |
| Number of Residues | 15 |
| Details | binding site for residues SHV X 1 and WFP X 2 |
| Chain | Residue |
| M | LEU24 |
| M | ASP27 |
| M | ILE29 |
| M | TYR63 |
| M | LEU115 |
| N | LEU49 |
| N | PHE50 |
| N | GLN52 |
| N | THR80 |
| N | HIS83 |
| X | SER3 |
| X | YCP5 |
| X | ALA6 |
| X | MP87 |
| X | HOH101 |
| site_id | AG7 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide WFP X 2 and SER X 3 |
| Chain | Residue |
| M | TYR63 |
| M | LEU115 |
| N | LEU49 |
| N | THR80 |
| N | HIS83 |
| X | SHV1 |
| X | PRO4 |
| X | YCP5 |
| X | ALA6 |
| X | MP87 |
| site_id | AG8 |
| Number of Residues | 13 |
| Details | binding site for residues SHV Y 1 and WFP Y 2 |
| Chain | Residue |
| S | LEU24 |
| S | ASP27 |
| S | ILE29 |
| S | TYR63 |
| S | MET190 |
| T | LEU49 |
| T | GLN52 |
| T | THR80 |
| T | HIS83 |
| Y | SER3 |
| Y | PRO4 |
| Y | YCP5 |
| Y | ALA6 |
| site_id | AG9 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide WFP Y 2 and SER Y 3 |
| Chain | Residue |
| S | TYR63 |
| S | MET190 |
| T | LEU49 |
| T | THR80 |
| T | HIS83 |
| Y | SHV1 |
| Y | PRO4 |
| Y | YCP5 |
| Y | ALA6 |
| Y | MP87 |
| site_id | AH1 |
| Number of Residues | 13 |
| Details | binding site for residues SHV Z 1 and WFP Z 2 |
| Chain | Residue |
| I | LEU49 |
| I | GLN52 |
| I | ALA53 |
| I | THR80 |
| I | HIS83 |
| T | ARG23 |
| T | LEU24 |
| T | ASP27 |
| T | ILE29 |
| T | TYR63 |
| Z | SER3 |
| Z | ALA6 |
| Z | HOH101 |
| site_id | AH2 |
| Number of Residues | 8 |
| Details | binding site for Di-peptide WFP Z 2 and SER Z 3 |
| Chain | Residue |
| I | LEU49 |
| I | THR80 |
| I | HIS83 |
| T | TYR63 |
| Z | SHV1 |
| Z | PRO4 |
| Z | ALA6 |
| Z | MP87 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444 |
| Chain | Residue | Details |
| A | SER98 | |
| L | SER98 | |
| M | SER98 | |
| N | SER98 | |
| S | SER98 | |
| T | SER98 | |
| B | SER98 | |
| C | SER98 | |
| D | SER98 | |
| E | SER98 | |
| F | SER98 | |
| G | SER98 | |
| I | SER98 | |
| K | SER98 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444 |
| Chain | Residue | Details |
| A | HIS123 | |
| L | HIS123 | |
| M | HIS123 | |
| N | HIS123 | |
| S | HIS123 | |
| T | HIS123 | |
| B | HIS123 | |
| C | HIS123 | |
| D | HIS123 | |
| E | HIS123 | |
| F | HIS123 | |
| G | HIS123 | |
| I | HIS123 | |
| K | HIS123 |
