1YJB
SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 35% DIMETHYLFORMAMIDE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 290 |
| Chain | Residue |
| A | GLN2 |
| A | ASP41 |
| A | LEU75 |
| A | ASN77 |
| A | ILE79 |
| A | VAL81 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 291 |
| Chain | Residue |
| A | ALA169 |
| A | TYR171 |
| A | VAL174 |
| A | HOH301 |
| site_id | CAT |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| A | ASP32 |
| A | HIS64 |
| A | SER221 |
| site_id | STR |
| Number of Residues | 6 |
| Details | OCCUPIED BY A CALCIUM ION. STRONG BINDING SITE. |
| Chain | Residue |
| A | GLN2 |
| A | ASP41 |
| A | LEU75 |
| A | ASN77 |
| A | ILE79 |
| A | VAL81 |
| site_id | WEA |
| Number of Residues | 5 |
| Details | OCCUPIED BY A CALCIUM ION AND A WATER MOLECULE. WEAK BINDING SITE. |
| Chain | Residue |
| A | ALA169 |
| A | TYR171 |
| A | VAL174 |
| A | GLU195 |
| A | ASP197 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH |
| Chain | Residue | Details |
| A | VAL28-HIS39 | |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA |
| Chain | Residue | Details |
| A | HIS64-ALA74 | |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG |
| Chain | Residue | Details |
| A | GLY219-GLY229 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP32 | |
| A | HIS64 | |
| A | SER221 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLN2 | |
| A | ASP41 | |
| A | LEU75 | |
| A | ASN77 | |
| A | ILE79 | |
| A | VAL81 | |
| A | ALA169 | |
| A | TYR171 | |
| A | VAL174 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| A | SER221 | |
| A | HIS64 | |
| A | ASP32 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 723 |
| Chain | Residue | Details |
| A | ASP32 | electrostatic interaction, electrostatic stabiliser |
| A | HIS64 | proton acceptor, proton donor |
| A | ASN155 | electrostatic interaction, electrostatic stabiliser |
| A | SER221 | nucleofuge, nucleophile, proton acceptor, proton donor |
