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 | 0030246 | molecular_function | carbohydrate binding |
| A | 0030248 | molecular_function | cellulose binding |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0030248 | molecular_function | cellulose binding |
Functional Information from PDB Data
| site_id | AA1 |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| A | ASP55 |
| A | ASP58 |
| A | GLU424 |
| site_id | AB1 |
| Number of Residues | 3 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| B | ASP55 |
| B | ASP58 |
| B | GLU424 |
| site_id | CA1 |
| Number of Residues | 5 |
| Details | CA BINDING SITE. |
| Chain | Residue |
| A | SER210 |
| A | GLY211 |
| A | ASP214 |
| A | GLU215 |
| A | ASP261 |
| site_id | CA2 |
| Number of Residues | 5 |
| Details | CA BINDING SITE. |
| Chain | Residue |
| B | ASP261 |
| B | SER210 |
| B | GLY211 |
| B | ASP214 |
| B | GLU215 |
| site_id | CA3 |
| Number of Residues | 5 |
| Details | CA BINDING SITE. |
| Chain | Residue |
| A | THR504 |
| A | ASP506 |
| A | ASP571 |
| A | ASN574 |
| A | ASP575 |
| site_id | CA4 |
| Number of Residues | 5 |
| Details | CA BINDING SITE. |
| Chain | Residue |
| B | THR504 |
| B | ASP506 |
| B | ASP571 |
| B | ASN574 |
| B | ASP575 |
Functional Information from PROSITE/UniProt
| site_id | PS00592 |
| Number of Residues | 27 |
| Details | GH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. YALGdNprnsSYVVGf....GnnPPrnPHHR |
| Chain | Residue | Details |
| A | TYR352-ARG378 | |
| site_id | PS00698 |
| Number of Residues | 19 |
| Details | GH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. YtDdrqdYvanEvAtdyNA |
| Chain | Residue | Details |
| A | TYR413-ALA431 | |
| site_id | PS60032 |
| Number of Residues | 18 |
| Details | GH9_1 Glycosyl hydrolases family 9 (GH9) active site signature 1. LtGGWYDAGDhvKFgFPM |
| Chain | Residue | Details |
| A | LEU49-MET66 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10140","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10059","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10060","evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9334746 |
| Chain | Residue | Details |
| A | ASP58 | |
| A | ASP55 | |
| A | GLU424 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9334746 |
| Chain | Residue | Details |
| B | ASP58 | |
| B | ASP55 | |
| B | GLU424 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 559 |
| Chain | Residue | Details |
| A | ASP55 | activator, electrostatic stabiliser, increase nucleophilicity |
| A | ASP58 | activator, increase nucleophilicity, proton acceptor, proton donor |
| A | TYR206 | electrostatic stabiliser |
| A | GLU424 | promote heterolysis, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 559 |
| Chain | Residue | Details |
| B | ASP55 | activator, electrostatic stabiliser, increase nucleophilicity |
| B | ASP58 | activator, increase nucleophilicity, proton acceptor, proton donor |
| B | TYR206 | electrostatic stabiliser |
| B | GLU424 | promote heterolysis, proton acceptor, proton donor |
