3M6A
Crystal structure of Bacillus subtilis Lon C-terminal domain
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 | 0005524 | molecular_function | ATP binding |
| A | 0006508 | biological_process | proteolysis |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0030163 | biological_process | protein catabolic process |
| B | 0004176 | molecular_function | ATP-dependent peptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006508 | biological_process | proteolysis |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0030163 | biological_process | protein catabolic process |
| C | 0004176 | molecular_function | ATP-dependent peptidase activity |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006508 | biological_process | proteolysis |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0030163 | biological_process | protein catabolic process |
| D | 0004176 | molecular_function | ATP-dependent peptidase activity |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006508 | biological_process | proteolysis |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0030163 | biological_process | protein catabolic process |
| E | 0004176 | molecular_function | ATP-dependent peptidase activity |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006508 | biological_process | proteolysis |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0030163 | biological_process | protein catabolic process |
| F | 0004176 | molecular_function | ATP-dependent peptidase activity |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006508 | biological_process | proteolysis |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0030163 | biological_process | protein catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP A 783 |
| Chain | Residue |
| A | PRO356 |
| A | LEU505 |
| A | LYS508 |
| A | VAL540 |
| A | GLU544 |
| A | GLY357 |
| A | VAL358 |
| A | GLY359 |
| A | LYS360 |
| A | THR361 |
| A | SER362 |
| A | TYR492 |
| A | ILE500 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP B 783 |
| Chain | Residue |
| B | HIS322 |
| B | HIS323 |
| B | PRO356 |
| B | GLY357 |
| B | VAL358 |
| B | GLY359 |
| B | LYS360 |
| B | THR361 |
| B | SER362 |
| B | TYR492 |
| B | ILE500 |
| B | VAL540 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP C 783 |
| Chain | Residue |
| C | HIS322 |
| C | HIS323 |
| C | GLY357 |
| C | VAL358 |
| C | GLY359 |
| C | LYS360 |
| C | THR361 |
| C | SER362 |
| C | TYR492 |
| C | ILE500 |
| C | VAL540 |
| C | GLU544 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP D 783 |
| Chain | Residue |
| D | HIS322 |
| D | HIS323 |
| D | PRO355 |
| D | PRO356 |
| D | GLY357 |
| D | VAL358 |
| D | GLY359 |
| D | LYS360 |
| D | THR361 |
| D | SER362 |
| D | TYR492 |
| D | ILE500 |
| D | VAL540 |
| D | GLU544 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP E 783 |
| Chain | Residue |
| E | GLU321 |
| E | HIS322 |
| E | HIS323 |
| E | PRO356 |
| E | GLY357 |
| E | VAL358 |
| E | GLY359 |
| E | LYS360 |
| E | THR361 |
| E | SER362 |
| E | TYR492 |
| E | ILE500 |
| E | LYS508 |
| E | VAL540 |
| E | GLU544 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP F 783 |
| Chain | Residue |
| F | HIS322 |
| F | HIS323 |
| F | PRO356 |
| F | GLY357 |
| F | VAL358 |
| F | GLY359 |
| F | LYS360 |
| F | THR361 |
| F | SER362 |
| F | TYR492 |
| F | ILE500 |
| F | VAL540 |
| F | GLU544 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01973 |
| Chain | Residue | Details |
| A | ALA677 | |
| E | LYS720 | |
| F | ALA677 | |
| F | LYS720 | |
| A | LYS720 | |
| B | ALA677 | |
| B | LYS720 | |
| C | ALA677 | |
| C | LYS720 | |
| D | ALA677 | |
| D | LYS720 | |
| E | ALA677 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY354 | |
| B | GLY354 | |
| C | GLY354 | |
| D | GLY354 | |
| E | GLY354 | |
| F | GLY354 |
