Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0016787 | molecular_function | hydrolase activity |
A | 0050525 | molecular_function | cutinase activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SXC A 215 |
Chain | Residue |
A | SER42 |
A | HIS188 |
A | LEU81 |
A | GLY82 |
A | ASN84 |
A | TYR119 |
A | SER120 |
A | GLN121 |
A | LEU182 |
A | ILE183 |
Functional Information from PROSITE/UniProt
site_id | PS00155 |
Number of Residues | 13 |
Details | CUTINASE_1 Cutinase, serine active site. PdAtLIaGGYSQG |
Chain | Residue | Details |
A | PRO110-GLY122 | |
site_id | PS00931 |
Number of Residues | 18 |
Details | CUTINASE_2 Cutinase, aspartate and histidine active sites. CktgDlVCtGSliVaapH |
Chain | Residue | Details |
A | CYS171-HIS188 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER120 | |
Chain | Residue | Details |
A | ASP175 | |
Chain | Residue | Details |
A | HIS188 | |
Chain | Residue | Details |
A | SER42 | |
Chain | Residue | Details |
A | GLN121 | |
Chain | Residue | Details |
A | GLY16 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1agy |
Chain | Residue | Details |
A | ASP175 | |
A | GLN121 | |
A | SER42 | |
A | SER120 | |
A | HIS188 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 631 |
Chain | Residue | Details |
A | SER42 | electrostatic stabiliser |
A | SER120 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
A | GLN121 | electrostatic stabiliser |
A | ASP175 | electrostatic stabiliser, increase basicity |
A | HIS188 | proton acceptor, proton donor |