3U9F
Structure of CATI in complex with chloramphenicol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0046677 | biological_process | response to antibiotic |
| E | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| E | 0016746 | molecular_function | acyltransferase activity |
| E | 0046677 | biological_process | response to antibiotic |
| F | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| F | 0016746 | molecular_function | acyltransferase activity |
| F | 0046677 | biological_process | response to antibiotic |
| G | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| G | 0016746 | molecular_function | acyltransferase activity |
| G | 0046677 | biological_process | response to antibiotic |
| H | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| H | 0016746 | molecular_function | acyltransferase activity |
| H | 0046677 | biological_process | response to antibiotic |
| I | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| I | 0016746 | molecular_function | acyltransferase activity |
| I | 0046677 | biological_process | response to antibiotic |
| J | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| J | 0016746 | molecular_function | acyltransferase activity |
| J | 0046677 | biological_process | response to antibiotic |
| K | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| K | 0016746 | molecular_function | acyltransferase activity |
| K | 0046677 | biological_process | response to antibiotic |
| L | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| L | 0016746 | molecular_function | acyltransferase activity |
| L | 0046677 | biological_process | response to antibiotic |
| M | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| M | 0016746 | molecular_function | acyltransferase activity |
| M | 0046677 | biological_process | response to antibiotic |
| N | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| N | 0016746 | molecular_function | acyltransferase activity |
| N | 0046677 | biological_process | response to antibiotic |
| O | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| O | 0016746 | molecular_function | acyltransferase activity |
| O | 0046677 | biological_process | response to antibiotic |
| P | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| P | 0016746 | molecular_function | acyltransferase activity |
| P | 0046677 | biological_process | response to antibiotic |
| R | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| R | 0016746 | molecular_function | acyltransferase activity |
| R | 0046677 | biological_process | response to antibiotic |
| S | 0008811 | molecular_function | chloramphenicol O-acetyltransferase activity |
| S | 0016746 | molecular_function | acyltransferase activity |
| S | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLM A 221 |
| Chain | Residue |
| A | SER104 |
| B | HIS193 |
| A | TYR133 |
| A | PHE134 |
| A | PHE144 |
| A | SER146 |
| A | PHE166 |
| A | HOH501 |
| B | PHE25 |
| B | ALA29 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLM B 221 |
| Chain | Residue |
| B | THR93 |
| B | SER104 |
| B | TYR133 |
| B | PHE134 |
| B | PHE144 |
| B | SER146 |
| B | LEU158 |
| B | VAL160 |
| B | PHE166 |
| B | VAL170 |
| C | PHE25 |
| C | HIS193 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLM C 221 |
| Chain | Residue |
| A | PHE25 |
| A | CYS31 |
| A | HIS193 |
| C | THR93 |
| C | PHE102 |
| C | SER104 |
| C | TYR133 |
| C | PHE134 |
| C | SER146 |
| C | VAL160 |
| C | PHE166 |
| C | HOH223 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLM D 221 |
| Chain | Residue |
| D | THR93 |
| D | PHE102 |
| D | SER104 |
| D | TYR133 |
| D | PHE144 |
| D | SER146 |
| D | PHE166 |
| D | VAL170 |
| E | PHE25 |
| E | ALA29 |
| E | HIS193 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CLM E 221 |
| Chain | Residue |
| E | PHE102 |
| E | SER104 |
| E | TYR133 |
| E | SER146 |
| E | VAL160 |
| E | PHE166 |
| F | PHE25 |
| F | HIS193 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLM F 221 |
| Chain | Residue |
| D | PHE25 |
| D | HIS193 |
| D | HOH647 |
| F | THR93 |
| F | SER104 |
| F | TYR133 |
| F | PHE134 |
| F | SER146 |
| F | VAL160 |
| F | PHE166 |
| F | HOH341 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLM G 221 |
| Chain | Residue |
| G | THR93 |
| G | PHE102 |
| G | SER104 |
| G | TYR133 |
| G | PHE144 |
| G | SER146 |
| G | PHE166 |
| H | PHE25 |
| H | ALA29 |
| H | CYS31 |
| H | HIS193 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CLM H 221 |
| Chain | Residue |
| H | SER104 |
| H | TYR133 |
| H | PHE144 |
| H | SER146 |
| H | VAL160 |
| H | HOH461 |
| I | PHE25 |
| I | HIS193 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLM I 221 |
| Chain | Residue |
| G | PHE25 |
| G | ALA29 |
| G | CYS31 |
| G | HIS193 |
| I | PHE102 |
| I | SER104 |
| I | TYR133 |
| I | PHE144 |
| I | SER146 |
| I | VAL160 |
| I | PHE166 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLM J 221 |
| Chain | Residue |
| J | PHE166 |
| J | VAL170 |
| J | HOH225 |
| J | HOH412 |
| K | HIS193 |
| J | SER104 |
| J | PHE134 |
| J | PHE144 |
| J | SER146 |
| J | VAL160 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLM K 221 |
| Chain | Residue |
| K | THR93 |
| K | PHE102 |
| K | SER104 |
| K | TYR133 |
| K | PHE134 |
| K | SER146 |
| K | VAL160 |
| K | PHE166 |
| L | PHE25 |
| L | HIS193 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLM L 221 |
| Chain | Residue |
| J | PHE25 |
| J | HIS193 |
| L | PHE102 |
| L | SER104 |
| L | TYR133 |
| L | PHE134 |
| L | PHE144 |
| L | SER146 |
| L | VAL160 |
| L | PHE166 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CLM M 221 |
| Chain | Residue |
| M | PHE102 |
| M | SER104 |
| M | TYR133 |
| M | PHE144 |
| M | SER146 |
| M | VAL160 |
| M | PHE166 |
| N | PHE25 |
| N | HIS193 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLM N 221 |
| Chain | Residue |
| N | THR93 |
| N | PHE102 |
| N | SER104 |
| N | TYR133 |
| N | SER146 |
| N | PHE166 |
| N | VAL170 |
| N | HOH226 |
| O | PHE25 |
| O | HIS193 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLM O 221 |
| Chain | Residue |
| M | PHE25 |
| M | HIS193 |
| O | THR93 |
| O | PHE102 |
| O | SER104 |
| O | TYR133 |
| O | PHE144 |
| O | SER146 |
| O | VAL160 |
| O | PHE166 |
| O | HOH568 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLM P 221 |
| Chain | Residue |
| P | THR93 |
| P | PHE102 |
| P | SER104 |
| P | TYR133 |
| P | SER146 |
| P | VAL160 |
| P | PHE166 |
| P | HOH1163 |
| R | PHE25 |
| R | ALA29 |
| R | HIS193 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CLM R 221 |
| Chain | Residue |
| R | PHE102 |
| R | SER104 |
| R | TYR133 |
| R | PHE144 |
| R | SER146 |
| R | VAL160 |
| S | PHE25 |
| S | CYS31 |
| S | HIS193 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CLM S 221 |
| Chain | Residue |
| P | PHE25 |
| P | HIS193 |
| S | PHE102 |
| S | SER104 |
| S | TYR133 |
| S | PHE144 |
| S | SER146 |
| S | VAL160 |
| S | PHE166 |
Functional Information from PROSITE/UniProt
| site_id | PS00100 |
| Number of Residues | 11 |
| Details | CAT Chloramphenicol acetyltransferase active site. QVHHAvcDGFH |
| Chain | Residue | Details |
| A | GLN190-HIS200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS193 | |
| J | HIS193 | |
| K | HIS193 | |
| L | HIS193 | |
| M | HIS193 | |
| N | HIS193 | |
| O | HIS193 | |
| P | HIS193 | |
| R | HIS193 | |
| S | HIS193 | |
| B | HIS193 | |
| C | HIS193 | |
| D | HIS193 | |
| E | HIS193 | |
| F | HIS193 | |
| G | HIS193 | |
| H | HIS193 | |
| I | HIS193 |
