2WNW
The crystal structure of SrfJ from salmonella typhimurium
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004348 | molecular_function | glucosylceramidase activity |
A | 0006665 | biological_process | sphingolipid metabolic process |
A | 0006680 | biological_process | glucosylceramide catabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046557 | molecular_function | glucan endo-1,6-beta-glucosidase activity |
B | 0004348 | molecular_function | glucosylceramidase activity |
B | 0006665 | biological_process | sphingolipid metabolic process |
B | 0006680 | biological_process | glucosylceramide catabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0046557 | molecular_function | glucan endo-1,6-beta-glucosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 1446 |
Chain | Residue |
A | ALA303 |
A | PO41447 |
B | ASN336 |
B | SER337 |
B | GLU338 |
B | TYR354 |
B | ASP355 |
B | ALA356 |
B | HOH2176 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 1446 |
Chain | Residue |
A | ARG405 |
A | ASP423 |
A | GLN444 |
A | HOH2175 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 1447 |
Chain | Residue |
B | ARG405 |
B | ASP423 |
B | GLN444 |
B | HOH2171 |
B | HOH2177 |
B | HOH2178 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 1447 |
Chain | Residue |
A | ASP302 |
A | GLY304 |
A | ARG308 |
A | HOH2182 |
B | SER337 |
B | GLU338 |
B | ASP355 |
B | PO41446 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 1448 |
Chain | Residue |
A | ASP273 |
A | HIS274 |
A | PHE275 |
A | SER276 |
A | HOH2183 |
A | HOH2184 |
B | SER387 |
B | SER388 |
B | GLU395 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 1449 |
Chain | Residue |
A | ASP94 |
A | PHE95 |
A | TRP144 |
A | ASN195 |
A | GLU196 |
A | TRP203 |
A | GLU294 |
A | TRP331 |
A | ASN346 |
A | HOH2086 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 1448 |
Chain | Residue |
B | ASP94 |
B | PHE95 |
B | TRP144 |
B | ASN195 |
B | GLU196 |
B | TRP203 |
B | GLU294 |
B | TRP331 |
B | ASN346 |
B | HOH2080 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 1449 |
Chain | Residue |
A | LEU109 |
A | GLN110 |
A | GLY112 |
A | ASP169 |
A | HOH2073 |
B | PRO223 |
B | ARG224 |
B | HOH2180 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DHDKDGLVDwaEL |
Chain | Residue | Details |
A | ASP239-LEU251 |