7CF6
Crystal structure of Beta-aspartyl dipeptidase from thermophilic keratin degrading Fervidobacterium islandicum AW-1 in complex with beta-Asp-Leu dipeptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | PHE11 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | TYR15 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | LEU106 |
| B | GLU107 |
| B | THR136 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | LYS292 |
| B | VAL300 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue FWO B 405 |
| Chain | Residue |
| B | GLU70 |
| B | THR99 |
| B | TYR130 |
| B | ARG163 |
| B | HIS224 |
| B | ARG227 |
| B | ASP285 |
| B | GLY288 |
| B | SER289 |
| B | LEU290 |
| B | PRO291 |
| B | ZN406 |
| B | ZN407 |
| B | HIS63 |
| B | GLY68 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 406 |
| Chain | Residue |
| B | TYR130 |
| B | GLU156 |
| B | HIS195 |
| B | HIS224 |
| B | FWO405 |
| B | ZN407 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 407 |
| Chain | Residue |
| B | HIS61 |
| B | HIS63 |
| B | GLU156 |
| B | ASP285 |
| B | FWO405 |
| B | ZN406 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | GLU44 |
| A | PHE373 |
| B | LYS376 |
| B | VAL379 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | GLU211 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | LYS230 |
| B | PHE207 |
| B | GLU211 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 406 |
| Chain | Residue |
| A | GLU156 |
| A | HIS195 |
| A | HIS224 |
| A | FWO405 |
| A | ZN407 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 407 |
| Chain | Residue |
| A | HIS61 |
| A | HIS63 |
| A | GLU156 |
| A | ASP285 |
| A | FWO405 |
| A | ZN406 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 401 |
| Chain | Residue |
| C | ARG241 |
| C | GLY242 |
| C | GOL403 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | GLY242 |
| C | ASN279 |
| C | ARG337 |
| C | GOL401 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | LYS340 |
| C | LEU341 |
| site_id | AD7 |
| Number of Residues | 15 |
| Details | binding site for residue FWO C 405 |
| Chain | Residue |
| C | HIS63 |
| C | GLY68 |
| C | GLU70 |
| C | TYR130 |
| C | GLU156 |
| C | ARG163 |
| C | HIS195 |
| C | HIS224 |
| C | GLY288 |
| C | SER289 |
| C | LEU290 |
| C | PRO291 |
| C | ZN406 |
| C | ZN407 |
| C | HOH517 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue ZN C 406 |
| Chain | Residue |
| C | HIS61 |
| C | HIS63 |
| C | GLU156 |
| C | HIS224 |
| C | ASP285 |
| C | FWO405 |
| C | ZN407 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 407 |
| Chain | Residue |
| C | TYR130 |
| C | GLU156 |
| C | HIS195 |
| C | HIS224 |
| C | FWO405 |
| C | ZN406 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue GOL D 401 |
| Chain | Residue |
| D | LEU341 |
| D | ASN342 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 403 |
| Chain | Residue |
| D | HIS61 |
| D | HIS63 |
| D | GLU156 |
| D | ASP285 |
| D | FWO402 |
| D | ZN404 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 404 |
| Chain | Residue |
| D | GLU156 |
| D | HIS195 |
| D | HIS224 |
| D | ZN403 |
| D | TYR130 |
| site_id | AE4 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide FWO A 405 and ARG A 227 |
| Chain | Residue |
| A | HIS63 |
| A | GLY68 |
| A | GLU70 |
| A | GLY98 |
| A | THR99 |
| A | TYR130 |
| A | GLU156 |
| A | ARG163 |
| A | HIS195 |
| A | VAL196 |
| A | GLY197 |
| A | HIS224 |
| A | MET225 |
| A | SER226 |
| A | SER228 |
| A | ASP285 |
| A | GLY288 |
| A | SER289 |
| A | LEU290 |
| A | PRO291 |
| A | ZN406 |
| A | ZN407 |
| site_id | AE5 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide FWO D 402 and ARG D 227 |
| Chain | Residue |
| D | HIS63 |
| D | GLU70 |
| D | THR99 |
| D | TYR130 |
| D | ARG163 |
| D | HIS195 |
| D | VAL196 |
| D | GLY197 |
| D | SER198 |
| D | HIS224 |
| D | MET225 |
| D | SER226 |
| D | SER228 |
| D | ASP285 |
| D | SER289 |
| D | ZN403 |
