Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008061 | molecular_function | chitin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1001 |
| Chain | Residue |
| A | GLY87 |
| A | PRO89 |
| A | ARG169 |
| A | HOH1034 |
| A | HOH1094 |
| A | HOH1270 |
| A | HOH1380 |
| A | HOH1561 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1002 |
| Chain | Residue |
| A | ASN113 |
| A | THR179 |
| A | ARG387 |
| A | TRP389 |
| A | GLU413 |
| A | GOL1011 |
| A | HOH1059 |
| A | HOH1748 |
| A | TRP82 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1003 |
| Chain | Residue |
| A | THR128 |
| A | ASP132 |
| A | THR133 |
| A | TRP134 |
| A | THR176 |
| A | ALA177 |
| A | ASP391 |
| A | LYS394 |
| A | HOH1052 |
| A | HOH1588 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1004 |
| Chain | Residue |
| A | ASP343 |
| A | GLY344 |
| A | ASN403 |
| A | LYS404 |
| A | ARG405 |
| A | SER424 |
| A | LYS425 |
| A | HOH1133 |
| A | HOH1359 |
| A | HOH1761 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1005 |
| Chain | Residue |
| A | ASN59 |
| A | ASN61 |
| A | ASP64 |
| A | VAL207 |
| A | PRO218 |
| A | LYS221 |
| A | HOH1169 |
| A | HOH1191 |
| A | HOH1755 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1006 |
| Chain | Residue |
| A | ASN83 |
| A | ASN110 |
| A | PRO112 |
| A | ASN113 |
| A | ASN381 |
| A | HOH1103 |
| A | HOH1195 |
| A | HOH1468 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1007 |
| Chain | Residue |
| A | TYR49 |
| A | PHE77 |
| A | ASP202 |
| A | GLU204 |
| A | ALA251 |
| A | MET277 |
| A | TYR279 |
| A | TRP433 |
| A | HOH1104 |
| A | HOH1230 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1008 |
| Chain | Residue |
| A | LEU33 |
| A | GLN34 |
| A | PRO35 |
| A | GLY253 |
| A | ALA254 |
| A | MET277 |
| A | TYR279 |
| A | ASP280 |
| A | HOH1759 |
| A | HOH1766 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 1009 |
| Chain | Residue |
| A | ILE138 |
| A | ASN143 |
| A | ASN146 |
| A | LYS193 |
| A | GLN347 |
| A | HOH1097 |
| A | HOH1198 |
| A | HOH1248 |
| A | HOH1309 |
| A | HOH1387 |
| A | HOH1465 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1010 |
| Chain | Residue |
| A | ASN195 |
| A | ASP242 |
| A | GLN347 |
| A | ALA348 |
| A | GLY349 |
| A | HOH1069 |
| A | HOH1152 |
| A | HOH1537 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 1011 |
| Chain | Residue |
| A | HOH1043 |
| A | HOH1411 |
| A | HOH1426 |
| A | HOH1742 |
| A | HOH1762 |
| A | HOH1767 |
| A | TRP82 |
| A | ASN83 |
| A | ARG387 |
| A | TYR388 |
| A | TRP389 |
| A | GOL1002 |
Functional Information from PROSITE/UniProt
| site_id | PS01095 |
| Number of Residues | 9 |
| Details | GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGVDLDwE |
| Chain | Residue | Details |
| A | PHE196-GLU204 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLU204 | |
| Chain | Residue | Details |
| A | ASP135 | |
| A | GLY162 | |
| A | TYR205 | |
| A | MET277 | |
| A | TRP433 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed Tews1997, 8103047 |
| Chain | Residue | Details |
| A | GLU204 | |
| A | ASP200 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 817 |
| Chain | Residue | Details |
| A | ASP200 | electrostatic stabiliser |
| A | ASP202 | electrostatic stabiliser, steric role |
| A | GLU204 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | TYR279 | electrostatic stabiliser, steric role |
