1WN3
Crystal structure of TT0310 protein from Thermus thermophilus HB8
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016289 | molecular_function | acyl-CoA hydrolase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016790 | molecular_function | thiolester hydrolase activity |
B | 0016289 | molecular_function | acyl-CoA hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016790 | molecular_function | thiolester hydrolase activity |
C | 0016289 | molecular_function | acyl-CoA hydrolase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016790 | molecular_function | thiolester hydrolase activity |
D | 0016289 | molecular_function | acyl-CoA hydrolase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016790 | molecular_function | thiolester hydrolase activity |
E | 0016289 | molecular_function | acyl-CoA hydrolase activity |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016790 | molecular_function | thiolester hydrolase activity |
F | 0016289 | molecular_function | acyl-CoA hydrolase activity |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016790 | molecular_function | thiolester hydrolase activity |
G | 0016289 | molecular_function | acyl-CoA hydrolase activity |
G | 0016787 | molecular_function | hydrolase activity |
G | 0016790 | molecular_function | thiolester hydrolase activity |
H | 0016289 | molecular_function | acyl-CoA hydrolase activity |
H | 0016787 | molecular_function | hydrolase activity |
H | 0016790 | molecular_function | thiolester hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 2001 |
Chain | Residue |
A | ARG67 |
B | ARG67 |
C | ARG67 |
D | ARG67 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL F 2002 |
Chain | Residue |
E | ARG67 |
F | ARG67 |
G | ARG67 |
H | ARG67 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT E 2007 |
Chain | Residue |
E | LEU9 |
E | ARG28 |
E | ASP30 |
E | HIS31 |
G | ALA8 |
E | ALA8 |
site_id | AC4 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE HXC C 2003 |
Chain | Residue |
A | ASP48 |
A | ALA52 |
A | ALA61 |
A | VAL62 |
A | ALA63 |
A | LEU64 |
A | PHE115 |
C | ASN33 |
C | HIS35 |
C | THR37 |
C | ALA38 |
C | GLY40 |
C | TYR70 |
C | PHE71 |
C | ARG72 |
C | PRO73 |
C | LYS105 |
C | HOH2010 |
C | HOH2025 |
C | HOH2026 |
C | HOH2027 |
C | HOH2029 |
C | HOH2073 |
C | HOH2075 |
D | SER90 |
D | ARG91 |
D | ARG92 |
D | HOH2030 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HXC D 2004 |
Chain | Residue |
B | ALA52 |
B | ALA61 |
B | VAL62 |
B | ALA63 |
B | LEU64 |
C | SER90 |
C | ARG91 |
C | ARG92 |
D | ASN33 |
D | HIS35 |
D | ALA38 |
D | GLY40 |
D | TYR70 |
D | PHE71 |
D | ARG72 |
D | PRO73 |
D | HOH2035 |
D | HOH2037 |
site_id | AC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE HXC E 2005 |
Chain | Residue |
A | HIS35 |
A | THR37 |
E | PHE51 |
E | ALA52 |
E | SER55 |
E | ASN56 |
E | ALA61 |
E | VAL62 |
E | ALA63 |
E | LEU64 |
E | VAL114 |
E | PHE115 |
E | LEU117 |
E | HOH2015 |
E | HOH2027 |
E | HOH2030 |
G | ASN33 |
G | HIS35 |
G | THR37 |
G | ALA38 |
G | TYR70 |
G | PHE71 |
G | ARG72 |
G | PRO73 |
H | SER90 |
H | ARG91 |
H | ARG92 |
H | THR93 |
site_id | AC7 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE HXC F 2006 |
Chain | Residue |
F | PHE115 |
F | LEU117 |
F | HOH2030 |
F | HOH2031 |
G | SER90 |
G | ARG91 |
G | ARG92 |
G | THR93 |
H | ASN33 |
H | HIS35 |
H | THR37 |
H | ALA38 |
H | TYR70 |
H | PHE71 |
H | ARG72 |
H | PRO73 |
H | HOH141 |
H | HOH161 |
B | HIS35 |
B | THR37 |
F | PHE51 |
F | ALA52 |
F | SER55 |
F | ASN56 |
F | ALA61 |
F | VAL62 |
F | ALA63 |
F | LEU64 |
F | VAL114 |