5AB7
Crystal structure of Trypanosoma brucei SCP2-thiolase like protein (TbSLP) in complex with malonyl-CoA.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| E | 0016746 | molecular_function | acyltransferase activity |
| E | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| F | 0016746 | molecular_function | acyltransferase activity |
| F | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE MLC A 1410 |
| Chain | Residue |
| A | GLY86 |
| A | ALA209 |
| A | ARG210 |
| A | ARG211 |
| A | TYR297 |
| A | CYS299 |
| A | PHE300 |
| A | LEU350 |
| A | TRP357 |
| A | ASN393 |
| A | GLY394 |
| A | GLY87 |
| A | GLY395 |
| A | HOH2043 |
| B | PHE59 |
| A | PHE125 |
| A | ILE143 |
| A | TYR188 |
| A | ARG197 |
| A | LEU205 |
| A | LEU206 |
| A | CYS208 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1409 |
| Chain | Residue |
| B | ARG135 |
| B | SER136 |
| B | GLY137 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MLC B 1410 |
| Chain | Residue |
| A | PHE59 |
| B | GLY87 |
| B | PHE125 |
| B | ILE143 |
| B | TYR188 |
| B | ARG197 |
| B | LEU205 |
| B | LEU206 |
| B | CYS208 |
| B | ALA209 |
| B | ARG210 |
| B | ARG211 |
| B | TYR297 |
| B | CYS299 |
| B | LEU350 |
| B | GLY394 |
| B | GLY395 |
| B | HOH2031 |
| B | HOH2046 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1411 |
| Chain | Residue |
| B | LYS386 |
| B | ARG387 |
| B | HOH2043 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1410 |
| Chain | Residue |
| C | HIS292 |
| C | LYS386 |
| C | ARG387 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1411 |
| Chain | Residue |
| C | ARG135 |
| C | GLY137 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1412 |
| Chain | Residue |
| C | ARG274 |
| C | HIS275 |
| C | ARG278 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MLC C 1413 |
| Chain | Residue |
| C | GLY86 |
| C | GLY87 |
| C | PHE125 |
| C | TYR188 |
| C | ARG197 |
| C | LEU205 |
| C | LEU206 |
| C | CYS208 |
| C | ALA209 |
| C | ARG210 |
| C | ARG211 |
| C | TYR297 |
| C | CYS299 |
| C | LEU350 |
| C | ASN393 |
| C | GLY394 |
| C | GLY395 |
| C | HOH2042 |
| C | HOH2048 |
| D | PHE59 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1410 |
| Chain | Residue |
| D | ARG135 |
| D | SER136 |
| D | GLY137 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE MLC D 1411 |
| Chain | Residue |
| D | GLY86 |
| D | GLY87 |
| D | SER122 |
| D | PHE125 |
| D | TYR188 |
| D | ARG197 |
| D | LEU205 |
| D | LEU206 |
| D | CYS208 |
| D | ALA209 |
| D | ARG210 |
| D | ARG211 |
| D | TYR297 |
| D | CYS299 |
| D | GLY394 |
| D | GLY395 |
| D | HOH2035 |
| D | HOH2043 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1412 |
| Chain | Residue |
| D | HIS292 |
| D | LYS386 |
| D | ARG387 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1413 |
| Chain | Residue |
| D | ARG13 |
| D | HIS179 |
| D | HIS347 |
| D | PHE353 |
| D | THR366 |
| D | GLU367 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1410 |
| Chain | Residue |
| E | ARG135 |
| E | SER136 |
| E | GLY137 |
| site_id | BC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MLC E 1411 |
| Chain | Residue |
| E | GLY86 |
| E | GLY87 |
| E | SER122 |
| E | PHE125 |
| E | ILE143 |
| E | PRO144 |
| E | TYR188 |
| E | ARG197 |
| E | LEU205 |
| E | LEU206 |
| E | CYS208 |
| E | ARG210 |
| E | ARG211 |
| E | TYR297 |
| E | CYS299 |
| E | PHE300 |
| E | GLY394 |
| E | GLY395 |
| E | HOH2036 |
| F | PHE59 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1412 |
| Chain | Residue |
| E | LYS386 |
| E | ARG387 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 F 1410 |
| Chain | Residue |
| A | HIS20 |
| F | HIS292 |
| F | LYS386 |
| F | ARG387 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 F 1411 |
| Chain | Residue |
| F | MET183 |
| F | CYS184 |
| F | GLN185 |
| F | LYS186 |
| site_id | BC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MLC F 1412 |
| Chain | Residue |
| E | PHE59 |
| F | GLY87 |
| F | ILE143 |
| F | TYR188 |
| F | ARG197 |
| F | LEU205 |
| F | LEU206 |
| F | CYS208 |
| F | ALA209 |
| F | ARG210 |
| F | ARG211 |
| F | TYR297 |
| F | CYS299 |
| F | LEU350 |
| F | ASN393 |
| F | GLY394 |
| F | GLY395 |
| F | HOH2024 |
| F | HOH2025 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 F 1413 |
| Chain | Residue |
| F | ARG13 |
| F | HIS179 |
| F | HIS347 |
| F | PHE353 |
| F | THR366 |
| F | GLU367 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1411 |
| Chain | Residue |
| A | LEU133 |
| A | ARG135 |
| A | SER136 |
| A | GLY137 |
