Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0005737 | cellular_component | cytoplasm |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
C | 0005737 | cellular_component | cytoplasm |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
D | 0005737 | cellular_component | cytoplasm |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PEG C 1489 |
Chain | Residue |
C | ILE240 |
C | HOH2122 |
D | GLU230 |
C | SER244 |
C | LEU263 |
C | GLN266 |
C | ALA267 |
C | LYS270 |
C | ASN272 |
C | HOH2071 |
C | HOH2088 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1490 |
Chain | Residue |
A | GLU230 |
A | ALA233 |
A | SER259 |
B | LYS270 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1491 |
Chain | Residue |
A | PHE237 |
A | LYS270 |
A | HOH2099 |
A | HOH2106 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1492 |
Chain | Residue |
A | ALA300 |
A | PHE336 |
A | LYS341 |
A | GLY354 |
A | ASN356 |
A | ALA429 |
A | TYR431 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL D 1490 |
Chain | Residue |
D | TYR170 |
D | ARG227 |
D | HOH2061 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 1493 |
Chain | Residue |
A | TYR170 |
A | ARG227 |
A | HOH2067 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 1489 |
Chain | Residue |
B | TYR170 |
B | ARG227 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 1490 |
Chain | Residue |
C | TYR170 |
C | ILE205 |
C | ARG227 |
C | HOH2046 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 1490 |
Chain | Residue |
B | ASP128 |
B | GLY464 |
B | GLY466 |
B | HOH2037 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG D 1491 |
Chain | Residue |
D | ASP128 |
D | GLY464 |
D | GLY466 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 1491 |
Chain | Residue |
C | ASP128 |
C | GLY464 |
C | GLY466 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 1494 |
Chain | Residue |
A | ASP128 |
A | GLY464 |
A | GLY466 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1495 |
Chain | Residue |
A | LYS254 |
A | ILE279 |
A | THR303 |
A | HOH2103 |
A | HOH2119 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER259 | |
B | SER259 | |
C | SER259 | |
D | SER259 | |
Chain | Residue | Details |
A | TYR431 | |
B | TYR431 | |
C | TYR431 | |
D | TYR431 | |