4HAP
Crystal Structure of a GH7 family cellobiohydrolase from Limnoria quadripunctata in complex with cellobiose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016162 | molecular_function | cellulose 1,4-beta-cellobiosidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030245 | biological_process | cellulose catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016162 | molecular_function | cellulose 1,4-beta-cellobiosidase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. GTVDSGSTLTVI |
| Chain | Residue | Details |
| A | GLY298-ILE309 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P62694 |
| Chain | Residue | Details |
| A | GLU233 | |
| B | GLU233 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P62694 |
| Chain | Residue | Details |
| A | GLU238 | |
| B | GLU238 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAQ |
| Chain | Residue | Details |
| A | TYR102 | |
| A | ASP124 | |
| A | LYS202 | |
| B | TYR102 | |
| B | ASP124 | |
| B | LYS202 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAP, ECO:0007744|PDB:4IPM |
| Chain | Residue | Details |
| A | ASP235 | |
| A | HIS249 | |
| A | TRP401 | |
| B | ASP235 | |
| B | HIS249 | |
| B | TRP401 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAQ, ECO:0007744|PDB:4IPM |
| Chain | Residue | Details |
| A | ARG271 | |
| B | ARG271 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23733951, ECO:0007744|PDB:4HAP, ECO:0007744|PDB:4HAQ, ECO:0007744|PDB:4IPM |
| Chain | Residue | Details |
| A | ASP279 | |
| A | ARG417 | |
| B | ASP279 | |
| B | ARG417 |
