3STJ
Crystal structure of the protease + PDZ1 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 |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0006508 | biological_process | proteolysis |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| I | 0004252 | molecular_function | serine-type endopeptidase activity |
| I | 0006508 | biological_process | proteolysis |
| J | 0004252 | molecular_function | serine-type endopeptidase activity |
| J | 0006508 | biological_process | proteolysis |
| K | 0004252 | molecular_function | serine-type endopeptidase activity |
| K | 0006508 | biological_process | proteolysis |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0006508 | biological_process | proteolysis |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:21685389 |
| Chain | Residue | Details |
| A | HIS82 | |
| D | HIS82 | |
| D | ASP112 | |
| D | SER187 | |
| E | HIS82 | |
| E | ASP112 | |
| E | SER187 | |
| F | HIS82 | |
| F | ASP112 | |
| F | SER187 | |
| G | HIS82 | |
| A | ASP112 | |
| G | ASP112 | |
| G | SER187 | |
| H | HIS82 | |
| H | ASP112 | |
| H | SER187 | |
| I | HIS82 | |
| I | ASP112 | |
| I | SER187 | |
| J | HIS82 | |
| J | ASP112 | |
| A | SER187 | |
| J | SER187 | |
| K | HIS82 | |
| K | ASP112 | |
| K | SER187 | |
| L | HIS82 | |
| L | ASP112 | |
| L | SER187 | |
| B | HIS82 | |
| B | ASP112 | |
| B | SER187 | |
| C | HIS82 | |
| C | ASP112 | |
| C | SER187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU32 | |
| D | GLU32 | |
| D | HIS82 | |
| D | ASP112 | |
| E | GLU32 | |
| E | HIS82 | |
| E | ASP112 | |
| F | GLU32 | |
| F | HIS82 | |
| F | ASP112 | |
| G | GLU32 | |
| A | HIS82 | |
| G | HIS82 | |
| G | ASP112 | |
| H | GLU32 | |
| H | HIS82 | |
| H | ASP112 | |
| I | GLU32 | |
| I | HIS82 | |
| I | ASP112 | |
| J | GLU32 | |
| J | HIS82 | |
| A | ASP112 | |
| J | ASP112 | |
| K | GLU32 | |
| K | HIS82 | |
| K | ASP112 | |
| L | GLU32 | |
| L | HIS82 | |
| L | ASP112 | |
| B | GLU32 | |
| B | HIS82 | |
| B | ASP112 | |
| C | GLU32 | |
| C | HIS82 | |
| C | ASP112 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21685389 |
| Chain | Residue | Details |
| A | GLY185 | |
| J | GLY185 | |
| K | GLY185 | |
| L | GLY185 | |
| B | GLY185 | |
| C | GLY185 | |
| D | GLY185 | |
| E | GLY185 | |
| F | GLY185 | |
| G | GLY185 | |
| H | GLY185 | |
| I | GLY185 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR203 | |
| E | LEU242 | |
| F | THR203 | |
| F | LEU242 | |
| G | THR203 | |
| G | LEU242 | |
| H | THR203 | |
| H | LEU242 | |
| I | THR203 | |
| I | LEU242 | |
| J | THR203 | |
| A | LEU242 | |
| J | LEU242 | |
| K | THR203 | |
| K | LEU242 | |
| L | THR203 | |
| L | LEU242 | |
| B | THR203 | |
| B | LEU242 | |
| C | THR203 | |
| C | LEU242 | |
| D | THR203 | |
| D | LEU242 | |
| E | THR203 |
