4GWA
Crystal Structure of a GH7 Family Cellobiohydrolase from Limnoria quadripunctata
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 PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | ASP80 |
A | HOH813 |
A | HOH881 |
A | HOH890 |
A | HOH994 |
A | HOH995 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | HOH752 |
A | HOH832 |
A | HOH983 |
A | GLU139 |
A | HOH697 |
A | HOH733 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 503 |
Chain | Residue |
A | HOH989 |
A | HOH990 |
A | HOH991 |
A | HOH992 |
A | HOH993 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 501 |
Chain | Residue |
B | GLU139 |
B | HOH744 |
B | HOH944 |
B | HOH945 |
B | HOH946 |
B | HOH947 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
A | HOH974 |
A | HOH980 |
B | HOH959 |
B | HOH960 |
B | HOH961 |
B | HOH1060 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 503 |
Chain | Residue |
A | HOH986 |
B | HOH954 |
B | HOH955 |
B | HOH956 |
B | HOH957 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 504 |
Chain | Residue |
A | GLU62 |
B | HOH634 |
B | HOH857 |
B | HOH951 |
B | HOH952 |
B | HOH953 |
B | HOH1092 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 505 |
Chain | Residue |
B | HOH674 |
B | HOH921 |
B | HOH941 |
B | HOH978 |
B | HOH988 |
B | HOH1090 |
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 |