6DL7
Human mitochondrial ClpP in complex with ONC201 (TIC10)
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue ONC A 301 |
Chain | Residue |
A | LEU79 |
G | HOH415 |
A | GLU82 |
A | HIS116 |
A | TYR118 |
A | TRP146 |
A | LEU170 |
G | SER108 |
G | THR135 |
G | TYR138 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue ONC B 301 |
Chain | Residue |
A | LEU104 |
A | SER108 |
A | THR135 |
A | TYR138 |
A | HOH409 |
B | LEU79 |
B | GLU82 |
B | HIS116 |
B | TYR118 |
B | TRP146 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue ONC C 301 |
Chain | Residue |
B | LEU104 |
B | SER108 |
B | THR135 |
B | HOH416 |
C | LEU79 |
C | GLU82 |
C | HIS116 |
C | TYR118 |
C | TRP146 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue ONC D 301 |
Chain | Residue |
C | LEU104 |
C | SER108 |
C | THR135 |
C | TYR138 |
C | HOH421 |
D | LEU79 |
D | GLU82 |
D | HIS116 |
D | TYR118 |
D | TRP146 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue ONC E 301 |
Chain | Residue |
D | LEU104 |
D | SER108 |
D | THR135 |
D | TYR138 |
D | HOH424 |
E | GLU82 |
E | HIS116 |
E | TYR118 |
E | TRP146 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue ONC F 301 |
Chain | Residue |
E | ILE100 |
E | LEU104 |
E | SER108 |
E | THR135 |
E | HOH424 |
F | LEU79 |
F | GLU82 |
F | HIS116 |
F | TYR118 |
F | TRP146 |
F | VAL148 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue ONC G 301 |
Chain | Residue |
F | SER108 |
F | THR135 |
F | TYR138 |
F | HOH426 |
G | LEU79 |
G | GLU82 |
G | HIS116 |
G | TYR118 |
G | TRP146 |
G | VAL148 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:11923310 |
Chain | Residue | Details |
A | SER153 | |
B | SER153 | |
C | SER153 | |
D | SER153 | |
E | SER153 | |
F | SER153 | |
G | SER153 |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | HIS178 | |
B | HIS178 | |
C | HIS178 | |
D | HIS178 | |
E | HIS178 | |
F | HIS178 | |
G | HIS178 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O88696 |
Chain | Residue | Details |
A | LYS200 | |
B | LYS200 | |
C | LYS200 | |
D | LYS200 | |
E | LYS200 | |
F | LYS200 | |
G | LYS200 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS211 | |
B | LYS211 | |
C | LYS211 | |
D | LYS211 | |
E | LYS211 | |
F | LYS211 | |
G | LYS211 |