3QNW
Caspase-6 in complex with Z-VAD-FMK inhibitor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008234 | molecular_function | cysteine-type peptidase activity |
B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008234 | molecular_function | cysteine-type peptidase activity |
C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008234 | molecular_function | cysteine-type peptidase activity |
D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008234 | molecular_function | cysteine-type peptidase activity |
E | 0004197 | molecular_function | cysteine-type endopeptidase activity |
E | 0006508 | biological_process | proteolysis |
E | 0008234 | molecular_function | cysteine-type peptidase activity |
F | 0004197 | molecular_function | cysteine-type endopeptidase activity |
F | 0006508 | biological_process | proteolysis |
F | 0008234 | molecular_function | cysteine-type peptidase activity |
G | 0004197 | molecular_function | cysteine-type endopeptidase activity |
G | 0006508 | biological_process | proteolysis |
G | 0008234 | molecular_function | cysteine-type peptidase activity |
H | 0004197 | molecular_function | cysteine-type endopeptidase activity |
H | 0006508 | biological_process | proteolysis |
H | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR CHAIN X OF Z-VAD-FMK |
Chain | Residue |
A | GLU123 |
B | TRP227 |
B | ALA269 |
B | LYS272 |
A | CYS163 |
B | ALA213 |
B | GLU214 |
B | GLY215 |
B | TYR216 |
B | TYR217 |
B | SER218 |
B | HIS219 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR CHAIN Y OF Z-VAD-FMK |
Chain | Residue |
C | ALA162 |
C | CYS163 |
D | VAL212 |
D | GLU214 |
D | GLY215 |
D | TYR216 |
D | TYR217 |
D | SER218 |
D | HIS219 |
D | TRP227 |
D | VAL261 |
D | LYS272 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR CHAIN Z OF Z-VAD-FMK |
Chain | Residue |
G | GLU123 |
G | CYS163 |
H | GLU214 |
H | GLY215 |
H | TYR216 |
H | TYR217 |
H | SER218 |
H | LYS272 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by NUAK1 and AMPK => ECO:0000269|PubMed:15273717, ECO:0000269|PubMed:22483120, ECO:0000269|PubMed:32029622 |
Chain | Residue | Details |
B | SER257 | |
D | SER257 | |
F | SER257 | |
H | SER257 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27911442 |
Chain | Residue | Details |
B | CYS264 | |
B | CYS277 | |
D | CYS264 | |
D | CYS277 | |
F | CYS264 | |
F | CYS277 | |
H | CYS264 | |
H | CYS277 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08738 |
Chain | Residue | Details |
A | SER79 | |
C | SER79 | |
E | SER79 | |
G | SER79 |