3V3K
Human caspase 9 in complex with bacterial effector protein
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 |
C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 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 |
G | 0004197 | molecular_function | cysteine-type endopeptidase activity |
G | 0006508 | biological_process | proteolysis |
G | 0008234 | molecular_function | cysteine-type peptidase activity |
I | 0004197 | molecular_function | cysteine-type endopeptidase activity |
I | 0006508 | biological_process | proteolysis |
I | 0008234 | molecular_function | cysteine-type peptidase activity |
K | 0004197 | molecular_function | cysteine-type endopeptidase activity |
K | 0006508 | biological_process | proteolysis |
K | 0008234 | molecular_function | cysteine-type peptidase activity |
M | 0004197 | molecular_function | cysteine-type endopeptidase activity |
M | 0006508 | biological_process | proteolysis |
M | 0008234 | molecular_function | cysteine-type peptidase activity |
O | 0004197 | molecular_function | cysteine-type endopeptidase activity |
O | 0006508 | biological_process | proteolysis |
O | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | HIS237 | |
A | CYS285 | |
C | HIS237 | |
C | CYS285 | |
E | HIS237 | |
E | CYS285 | |
G | HIS237 | |
G | CYS285 | |
I | HIS237 | |
I | CYS285 | |
K | HIS237 | |
K | CYS285 | |
M | HIS237 | |
M | CYS285 | |
O | HIS237 | |
O | CYS285 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine; by ABL1 => ECO:0000269|PubMed:15657060 |
Chain | Residue | Details |
A | TYR153 | |
C | TYR153 | |
E | TYR153 | |
G | TYR153 | |
I | TYR153 | |
K | TYR153 | |
M | TYR153 | |
O | TYR153 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER298 | |
C | SER298 | |
E | SER298 | |
G | SER296 | |
I | SER298 | |
K | SER298 | |
M | SER298 | |
O | SER298 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER298 | |
C | SER298 | |
E | SER298 | |
G | SER296 | |
I | SER298 | |
K | SER298 | |
M | SER298 | |
O | SER298 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER298 | |
C | SER298 | |
E | SER298 | |
G | SER296 | |
I | SER298 | |
K | SER298 | |
M | SER298 | |
O | SER298 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120 |
Chain | Residue | Details |
A | ARG341 | |
C | ARG341 | |
E | ARG341 | |
G | ARG341 | |
I | ARG341 | |
K | ARG341 | |
M | ARG341 | |
O | ARG341 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
A | ARG177 | electrostatic stabiliser |
A | HIS237 | proton acceptor, proton donor |
A | GLY238 | electrostatic stabiliser |
A | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
C | ARG177 | electrostatic stabiliser |
C | HIS237 | proton acceptor, proton donor |
C | GLY238 | electrostatic stabiliser |
C | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
E | ARG177 | electrostatic stabiliser |
E | HIS237 | proton acceptor, proton donor |
E | GLY238 | electrostatic stabiliser |
E | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
G | ARG177 | electrostatic stabiliser |
G | HIS237 | proton acceptor, proton donor |
G | GLY238 | electrostatic stabiliser |
G | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA5 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
I | ARG177 | electrostatic stabiliser |
I | HIS237 | proton acceptor, proton donor |
I | GLY238 | electrostatic stabiliser |
I | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA6 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
K | ARG177 | electrostatic stabiliser |
K | HIS237 | proton acceptor, proton donor |
K | GLY238 | electrostatic stabiliser |
K | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA7 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
M | ARG177 | electrostatic stabiliser |
M | HIS237 | proton acceptor, proton donor |
M | GLY238 | electrostatic stabiliser |
M | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |
site_id | MCSA8 |
Number of Residues | 4 |
Details | M-CSA 816 |
Chain | Residue | Details |
O | ARG177 | electrostatic stabiliser |
O | HIS237 | proton acceptor, proton donor |
O | GLY238 | electrostatic stabiliser |
O | CYS285 | nucleofuge, nucleophile, proton acceptor, proton donor |