7KSL
Substrate-free human mitochondrial LONP1
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 |
| 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 | 8 |
| Details | binding site for residue ADP C 1000 |
| Chain | Residue |
| C | TYR492 |
| C | GLY526 |
| C | VAL527 |
| C | GLY528 |
| C | LYS529 |
| C | THR530 |
| C | SER531 |
| C | TYR661 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue ADP B 1000 |
| Chain | Residue |
| B | TYR492 |
| B | GLY526 |
| B | VAL527 |
| B | GLY528 |
| B | LYS529 |
| B | THR530 |
| B | SER531 |
| B | TYR661 |
| B | ILE669 |
| B | TYR673 |
| B | GLN677 |
| B | VAL709 |
| B | ARG710 |
| B | GLN713 |
| B | HIS491 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue ADP A 1000 |
| Chain | Residue |
| A | HIS491 |
| A | TYR492 |
| A | GLY526 |
| A | VAL527 |
| A | GLY528 |
| A | LYS529 |
| A | THR530 |
| A | TYR661 |
| A | ILE669 |
| A | TYR673 |
| A | VAL709 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue ADP F 1000 |
| Chain | Residue |
| F | HIS491 |
| F | TYR492 |
| F | GLY526 |
| F | VAL527 |
| F | GLY528 |
| F | LYS529 |
| F | THR530 |
| F | TYR661 |
| F | ILE669 |
| F | VAL709 |
| F | GLN713 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue ADP E 1000 |
| Chain | Residue |
| E | TYR492 |
| E | GLY526 |
| E | VAL527 |
| E | GLY528 |
| E | LYS529 |
| E | THR530 |
| E | TYR661 |
| E | ILE669 |
| E | VAL709 |
| E | ARG710 |
Functional Information from PROSITE/UniProt
| site_id | PS01046 |
| Number of Residues | 9 |
| Details | LON_SER ATP-dependent serine proteases, lon family, serine active site. DGPSAGCTI |
| Chain | Residue | Details |
| C | ASP852-ILE860 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03120","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 35 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03120","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
