3STI
Crystal structure of the protease domain of DegQ from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:21685389 |
| Chain | Residue | Details |
| A | HIS82 | |
| A | ASP112 | |
| A | SER187 | |
| B | HIS82 | |
| B | ASP112 | |
| B | SER187 | |
| C | HIS82 | |
| C | ASP112 | |
| C | SER187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU32 | |
| A | HIS82 | |
| A | ASP112 | |
| B | GLU32 | |
| B | HIS82 | |
| B | ASP112 | |
| C | GLU32 | |
| C | HIS82 | |
| C | ASP112 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21685389 |
| Chain | Residue | Details |
| A | GLY185 | |
| B | GLY185 | |
| C | GLY185 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR203 | |
| B | THR203 | |
| C | THR203 |
