4YPL
Crystal structure of a hexameric LonA protease bound to three ADPs
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 | 11 |
Details | binding site for residue 4KZ A 801 |
Chain | Residue |
A | ALA601 |
A | ALA679 |
A | LYS721 |
A | TRP602 |
A | LEU610 |
A | MET633 |
A | LYS674 |
A | ASP675 |
A | GLY676 |
A | PRO677 |
A | SER678 |
site_id | AC2 |
Number of Residues | 16 |
Details | binding site for residue ADP B 801 |
Chain | Residue |
B | HIS319 |
B | TYR320 |
B | LEU322 |
B | PRO357 |
B | GLY358 |
B | VAL359 |
B | GLY360 |
B | LYS361 |
B | THR362 |
B | SER363 |
B | TYR493 |
B | ILE501 |
B | LYS509 |
B | VAL540 |
B | ARG541 |
B | GLU544 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue ADP F 801 |
Chain | Residue |
F | HIS319 |
F | TYR320 |
F | GLY358 |
F | VAL359 |
F | GLY360 |
F | LYS361 |
F | THR362 |
F | SER363 |
F | TYR493 |
F | ILE501 |
F | LEU506 |
F | VAL540 |
F | ARG541 |
F | GLU544 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue ADP D 801 |
Chain | Residue |
D | HIS319 |
D | TYR320 |
D | GLY358 |
D | VAL359 |
D | GLY360 |
D | LYS361 |
D | THR362 |
D | SER363 |
D | TYR493 |
D | ILE501 |
D | TYR505 |
D | VAL540 |
D | ARG541 |
D | GLU544 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for Di-peptide 4KZ B 802 and SER B 678 |
Chain | Residue |
B | LEU600 |
B | ALA601 |
B | TRP602 |
B | THR603 |
B | LEU610 |
B | MET633 |
B | LYS674 |
B | ASP675 |
B | GLY676 |
B | PRO677 |
B | ALA679 |
B | GLY680 |
B | THR703 |
B | GLY704 |
B | LYS721 |
site_id | AC6 |
Number of Residues | 18 |
Details | binding site for Di-peptide 4KZ C 801 and SER C 678 |
Chain | Residue |
C | LEU600 |
C | ALA601 |
C | TRP602 |
C | THR603 |
C | THR608 |
C | LEU610 |
C | MET633 |
C | PRO673 |
C | LYS674 |
C | ASP675 |
C | GLY676 |
C | PRO677 |
C | ALA679 |
C | GLY680 |
C | THR703 |
C | GLY704 |
C | GLU705 |
C | LYS721 |
site_id | AC7 |
Number of Residues | 15 |
Details | binding site for Di-peptide 4KZ D 802 and SER D 678 |
Chain | Residue |
D | GLY680 |
D | THR703 |
D | GLY704 |
D | LYS721 |
D | ALA601 |
D | TRP602 |
D | THR603 |
D | THR608 |
D | MET633 |
D | PRO673 |
D | LYS674 |
D | ASP675 |
D | GLY676 |
D | PRO677 |
D | ALA679 |
site_id | AC8 |
Number of Residues | 16 |
Details | binding site for Di-peptide 4KZ E 801 and SER E 678 |
Chain | Residue |
E | LEU600 |
E | ALA601 |
E | TRP602 |
E | THR603 |
E | MET633 |
E | THR672 |
E | PRO673 |
E | LYS674 |
E | ASP675 |
E | GLY676 |
E | PRO677 |
E | ALA679 |
E | GLY680 |
E | THR703 |
E | GLY704 |
E | LYS721 |
site_id | AC9 |
Number of Residues | 14 |
Details | binding site for Di-peptide 4KZ F 802 and SER F 678 |
Chain | Residue |
F | LEU600 |
F | ALA601 |
F | TRP602 |
F | THR608 |
F | LYS674 |
F | ASP675 |
F | GLY676 |
F | PRO677 |
F | ALA679 |
F | GLY680 |
F | THR703 |
F | GLY704 |
F | ILE715 |
F | LYS721 |
Functional Information from PROSITE/UniProt
site_id | PS01046 |
Number of Residues | 9 |
Details | LON_SER ATP-dependent serine proteases, lon family, serine active site. DGPSAGITM |
Chain | Residue | Details |
A | ASP675-MET683 |