3KVU
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA FlK - T42S mutant in complex with Acetyl-CoA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016289 | molecular_function | acyl-CoA hydrolase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0016289 | molecular_function | acyl-CoA hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
C | 0016289 | molecular_function | acyl-CoA hydrolase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0042803 | molecular_function | protein homodimerization activity |
D | 0016289 | molecular_function | acyl-CoA hydrolase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ACO A 201 |
Chain | Residue |
A | VAL23 |
B | GLY69 |
A | ALA41 |
A | SER42 |
A | HIS76 |
A | THR77 |
A | ALA78 |
A | ALA79 |
A | HOH414 |
B | GLU50 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ACO B 200 |
Chain | Residue |
A | GLU50 |
A | GLY69 |
A | ALA121 |
A | ILE123 |
A | LYS127 |
A | PHE128 |
A | LYS131 |
B | VAL23 |
B | VAL39 |
B | PHE40 |
B | ALA41 |
B | SER42 |
B | HIS76 |
B | THR77 |
B | ALA78 |
B | ALA79 |
B | ASP111 |
B | HOH365 |
B | HOH453 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ACO D 202 |
Chain | Residue |
C | GLU50 |
C | LEU68 |
C | GLY69 |
C | ARG99 |
C | ALA121 |
D | SER42 |
D | HIS76 |
D | THR77 |
D | ALA78 |
D | ALA79 |
D | HOH405 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | SER42 | |
D | SER42 | |
D | GLU50 | |
D | HIS76 | |
A | GLU50 | |
A | HIS76 | |
B | SER42 | |
B | GLU50 | |
B | HIS76 | |
C | SER42 | |
C | GLU50 | |
C | HIS76 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | PHE40 | |
A | HIS76 | |
B | PHE40 | |
B | HIS76 | |
C | PHE40 | |
C | HIS76 | |
D | PHE40 | |
D | HIS76 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20430898, ECO:0000269|PubMed:20836570 |
Chain | Residue | Details |
A | GLY69 | |
A | ARG120 | |
B | GLY69 | |
B | ARG120 | |
C | GLY69 | |
C | ARG120 | |
D | GLY69 | |
D | ARG120 |