7D6Q
Crystal structure of the Stx2a
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017148 | biological_process | negative regulation of translation |
A | 0030598 | molecular_function | rRNA N-glycosylase activity |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0090729 | molecular_function | toxin activity |
B | 0005576 | cellular_component | extracellular region |
B | 0019836 | biological_process | hemolysis by symbiont of host erythrocytes |
C | 0005576 | cellular_component | extracellular region |
C | 0019836 | biological_process | hemolysis by symbiont of host erythrocytes |
D | 0005576 | cellular_component | extracellular region |
D | 0019836 | biological_process | hemolysis by symbiont of host erythrocytes |
E | 0005576 | cellular_component | extracellular region |
E | 0019836 | biological_process | hemolysis by symbiont of host erythrocytes |
F | 0005576 | cellular_component | extracellular region |
F | 0019836 | biological_process | hemolysis by symbiont of host erythrocytes |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue 1PS B 101 |
Chain | Residue |
B | ASN14 |
B | ASP16 |
B | THR18 |
B | TRP29 |
B | HOH211 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue 1PS C 101 |
Chain | Residue |
C | HOH205 |
C | HOH224 |
D | SER58 |
C | GLU15 |
C | ASP16 |
C | THR18 |
C | TRP29 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue 1PS D 101 |
Chain | Residue |
C | SER58 |
D | ASN14 |
D | GLU15 |
D | ASP16 |
D | THR18 |
D | TRP29 |
D | HOH202 |
D | HOH222 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue 1PS F 101 |
Chain | Residue |
F | ASN14 |
F | ASP16 |
F | THR18 |
F | TRP29 |
F | HOH208 |
Functional Information from PROSITE/UniProt
site_id | PS00275 |
Number of Residues | 17 |
Details | SHIGA_RICIN Shiga/ricin ribosomal inactivating toxins active site signature. VtVTaEALRFRqIQreF |
Chain | Residue | Details |
A | VAL162-PHE178 |