6H23
Crystal structure of the hClpP Y118A mutant with an activating small molecule
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 | 0006508 | biological_process | proteolysis |
| B | 0004176 | molecular_function | ATP-dependent peptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0004176 | molecular_function | ATP-dependent peptidase activity |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| D | 0004176 | molecular_function | ATP-dependent peptidase activity |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| E | 0004176 | molecular_function | ATP-dependent peptidase activity |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| F | 0004176 | molecular_function | ATP-dependent peptidase activity |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| G | 0004176 | molecular_function | ATP-dependent peptidase activity |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0006508 | biological_process | proteolysis |
| H | 0004176 | molecular_function | ATP-dependent peptidase activity |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| I | 0004176 | molecular_function | ATP-dependent peptidase activity |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0006508 | biological_process | proteolysis |
| J | 0004176 | molecular_function | ATP-dependent peptidase activity |
| J | 0004252 | molecular_function | serine-type endopeptidase activity |
| J | 0006508 | biological_process | proteolysis |
| K | 0004176 | molecular_function | ATP-dependent peptidase activity |
| K | 0004252 | molecular_function | serine-type endopeptidase activity |
| K | 0006508 | biological_process | proteolysis |
| L | 0004176 | molecular_function | ATP-dependent peptidase activity |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0006508 | biological_process | proteolysis |
| M | 0004176 | molecular_function | ATP-dependent peptidase activity |
| M | 0004252 | molecular_function | serine-type endopeptidase activity |
| M | 0006508 | biological_process | proteolysis |
| N | 0004176 | molecular_function | ATP-dependent peptidase activity |
| N | 0004252 | molecular_function | serine-type endopeptidase activity |
| N | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue FJT A 301 |
| Chain | Residue |
| A | ALA101 |
| B | VAL148 |
| A | LEU104 |
| A | PHE105 |
| A | SER108 |
| A | TYR138 |
| B | LEU79 |
| B | GLU82 |
| B | ILE84 |
| B | TRP146 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLN194 |
| A | ALA195 |
| H | GLN179 |
| H | LYS202 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue FJT B 301 |
| Chain | Residue |
| B | ILE100 |
| B | ALA101 |
| B | LEU104 |
| B | PHE105 |
| B | GLN107 |
| B | SER108 |
| B | THR135 |
| B | TYR138 |
| C | ARG78 |
| C | LEU79 |
| C | GLU82 |
| C | ILE84 |
| C | TRP146 |
| C | VAL148 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue FJT D 301 |
| Chain | Residue |
| C | ILE100 |
| C | ALA101 |
| C | LEU104 |
| C | PHE105 |
| C | SER108 |
| C | TYR138 |
| D | LEU79 |
| D | GLU82 |
| D | ILE84 |
| D | TRP146 |
| D | VAL148 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue FJT D 302 |
| Chain | Residue |
| D | ILE100 |
| D | ALA101 |
| D | LEU104 |
| D | PHE105 |
| D | SER108 |
| D | TYR138 |
| E | ARG78 |
| E | LEU79 |
| E | GLU82 |
| E | TRP146 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue FJT E 301 |
| Chain | Residue |
| E | ILE100 |
| E | ALA101 |
| E | LEU104 |
| E | PHE105 |
| E | SER108 |
| E | TYR138 |
| F | ARG78 |
| F | LEU79 |
| F | GLU82 |
| F | ILE84 |
| F | TRP146 |
| F | VAL148 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO E 302 |
| Chain | Residue |
| E | LYS202 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue FJT F 301 |
| Chain | Residue |
| F | ALA101 |
| F | LEU104 |
| F | PHE105 |
| F | SER108 |
| F | TYR138 |
| G | LEU79 |
| G | GLU82 |
| G | ILE84 |
| G | TRP146 |
| G | VAL148 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO F 302 |
| Chain | Residue |
| F | GLN179 |
| F | ILE198 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue FJT G 301 |
| Chain | Residue |
| A | LEU79 |
| A | GLU82 |
| A | ILE84 |
| A | TRP146 |
| G | ILE100 |
| G | ALA101 |
| G | LEU104 |
| G | PHE105 |
| G | SER108 |
| G | TYR138 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue FJT H 301 |
| Chain | Residue |
| H | ARG78 |
| H | LEU79 |
| H | GLU82 |
| H | TRP146 |
| H | VAL148 |
| N | ILE100 |
| N | ALA101 |
| N | LEU104 |
| N | PHE105 |
| N | SER108 |
| N | TYR138 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue FJT H 302 |
| Chain | Residue |
| H | GLN107 |
| H | SER108 |
| H | TYR138 |
| I | LEU79 |
| I | GLU82 |
| I | ILE84 |
| H | ILE100 |
| H | ALA101 |
| H | LEU104 |
| H | PHE105 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue FJT J 301 |
| Chain | Residue |
| I | ILE100 |
| I | ALA101 |
| I | LEU104 |
| I | PHE105 |
| I | SER108 |
| I | TYR138 |
| J | ARG78 |
| J | LEU79 |
| J | GLU82 |
| J | TRP146 |
| J | VAL148 |
| site_id | AD5 |
| Number of Residues | 13 |
| Details | binding site for residue FJT K 301 |
| Chain | Residue |
| J | ALA101 |
| J | LEU104 |
| J | PHE105 |
| J | SER108 |
| J | TYR138 |
| K | ARG78 |
| K | LEU79 |
| K | GLU82 |
| K | ILE84 |
| K | HIS116 |
| K | ALA118 |
| K | TRP146 |
| K | VAL148 |
| site_id | AD6 |
| Number of Residues | 13 |
| Details | binding site for residue FJT L 301 |
| Chain | Residue |
| K | LEU104 |
| K | PHE105 |
| K | SER108 |
| K | THR135 |
| K | TYR138 |
| L | ARG78 |
| L | LEU79 |
| L | GLU82 |
| L | ILE84 |
| L | ALA118 |
| L | TRP146 |
| L | VAL148 |
| L | LEU170 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue FJT M 301 |
| Chain | Residue |
| L | ILE100 |
| L | LEU104 |
| L | PHE105 |
| L | GLN107 |
| L | SER108 |
| M | LEU79 |
| M | GLU82 |
| M | ILE84 |
| M | TRP146 |
| M | VAL148 |
| site_id | AD8 |
| Number of Residues | 10 |
| Details | binding site for residue FJT M 302 |
| Chain | Residue |
| M | ALA101 |
| M | LEU104 |
| M | PHE105 |
| M | SER108 |
| M | TYR138 |
| N | LEU79 |
| N | GLU82 |
| N | ILE84 |
| N | TRP146 |
| N | VAL148 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO N 301 |
| Chain | Residue |
| N | GLN179 |
| N | ILE198 |
| N | LYS202 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:11923310 |
| Chain | Residue | Details |
| A | SER153 | |
| J | SER153 | |
| K | SER153 | |
| L | SER153 | |
| M | SER153 | |
| N | SER153 | |
| B | SER153 | |
| C | SER153 | |
| D | SER153 | |
| E | SER153 | |
| F | SER153 | |
| G | SER153 | |
| H | SER153 | |
| I | SER153 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS178 | |
| J | HIS178 | |
| K | HIS178 | |
| L | HIS178 | |
| M | HIS178 | |
| N | HIS178 | |
| B | HIS178 | |
| C | HIS178 | |
| D | HIS178 | |
| E | HIS178 | |
| F | HIS178 | |
| G | HIS178 | |
| H | HIS178 | |
| I | HIS178 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O88696 |
| Chain | Residue | Details |
| A | LYS200 | |
| J | LYS200 | |
| K | LYS200 | |
| L | LYS200 | |
| M | LYS200 | |
| N | LYS200 | |
| B | LYS200 | |
| C | LYS200 | |
| D | LYS200 | |
| E | LYS200 | |
| F | LYS200 | |
| G | LYS200 | |
| H | LYS200 | |
| I | LYS200 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS211 | |
| J | LYS211 | |
| K | LYS211 | |
| L | LYS211 | |
| M | LYS211 | |
| N | LYS211 | |
| B | LYS211 | |
| C | LYS211 | |
| D | LYS211 | |
| E | LYS211 | |
| F | LYS211 | |
| G | LYS211 | |
| H | LYS211 | |
| I | LYS211 |
