1GDN
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 | HOH1028 |
A | HOH1227 |
A | HOH1250 |
A | HOH1298 |
A | HOH1303 |
A | HOH1321 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 243 |
Chain | Residue |
A | ASP129 |
A | PRO130 |
A | VAL131 |
A | ALA132 |
A | SER164 |
A | ARG165 |
A | HOH1038 |
A | HOH1053 |
A | HOH1075 |
A | HOH1209 |
A | HOH1374 |
site_id | AC3 |
Number of Residues | 13 |
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 | HOH1042 |
A | HOH1068 |
A | HOH1132 |
A | HOH1309 |
A | HOH1361 |
A | HOH1411 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 245 |
Chain | Residue |
A | ALA24 |
A | GLY25 |
A | ASP26 |
A | SER70 |
A | ASN117 |
A | HOH1009 |
A | HOH1023 |
A | HOH1083 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 246 |
Chain | Residue |
A | ASP26 |
A | PHE27 |
A | GLY59 |
A | TYR59 |
A | VAL200 |
A | ASN203 |
A | HOH1032 |
A | HOH1357 |
site_id | AC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR CHAIN B OF GLY-ALA-LYS |
Chain | Residue |
A | HIS57 |
A | ASP189 |
A | SER190 |
A | CYS191 |
A | GLN192 |
A | GLY193 |
A | ASP194 |
A | SER195 |
A | SER214 |
A | TRP215 |
A | GLY216 |
A | HOH2104 |
B | HOH1289 |
B | HOH2003 |
B | HOH2004 |
B | HOH2005 |
B | HOH2006 |
B | HOH2101 |
B | HOH2102 |
B | HOH2103 |
B | HOH2201 |
B | HOH2202 |
B | HOH2204 |
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 |