1FY4
FUSARIUM OXYSPORUM TRYPSIN AT ATOMIC RESOLUTION
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 247 |
| Chain | Residue |
| A | PRO40 |
| A | ARG73 |
| A | SER93 |
| A | HOH1047 |
| A | HOH1159 |
| A | HOH1175 |
| A | HOH1212 |
| A | HOH1226 |
| A | HOH1352 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 243 |
| Chain | Residue |
| A | ASP129 |
| A | PRO130 |
| A | VAL131 |
| A | ALA132 |
| A | SER164 |
| A | ARG165 |
| A | HOH1041 |
| A | HOH1042 |
| A | HOH1081 |
| A | HOH1179 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 244 |
| Chain | Residue |
| A | SER21 |
| A | GLY127 |
| A | ASP129 |
| A | ASN154 |
| A | ARG165 |
| A | ASN178 |
| A | HOH1015 |
| A | HOH1076 |
| A | HOH1341 |
| A | HOH1363 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 245 |
| Chain | Residue |
| A | ALA24 |
| A | GLY25 |
| A | ASP26 |
| A | PHE27 |
| A | SER70 |
| A | ASN117 |
| A | HOH1011 |
| A | HOH1024 |
| A | HOH1070 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 246 |
| Chain | Residue |
| A | ASP26 |
| A | PHE27 |
| A | GLY59 |
| A | TYR59 |
| A | VAL200 |
| A | ASN203 |
| A | HOH1040 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| A | HIS57 | |
| A | ASP102 | |
| A | SER195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | SITE: Required for specificity |
| Chain | Residue | Details |
| A | ASP189 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | HIS57 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY196 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY193 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | GLY193 | |
| A | HIS57 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 | |
| A | GLY196 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 173 |
| Chain | Residue | Details |
| A | HIS57 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP102 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | GLN192 | electrostatic stabiliser, hydrogen bond donor, transition state stabiliser |
| A | GLY193 | electrostatic stabiliser, hydrogen bond donor, transition state stabiliser |
| A | ASP194 | electrostatic stabiliser, hydrogen bond donor, transition state stabiliser |
| A | SER195 | electrostatic stabiliser, transition state stabiliser |
