2NYG
Crystal structure of YokD protein from Bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008080 | molecular_function | N-acetyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008080 | molecular_function | N-acetyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0008080 | molecular_function | N-acetyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0008080 | molecular_function | N-acetyltransferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0046677 | biological_process | response to antibiotic |
| E | 0008080 | molecular_function | N-acetyltransferase activity |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016746 | molecular_function | acyltransferase activity |
| E | 0046677 | biological_process | response to antibiotic |
| F | 0008080 | molecular_function | N-acetyltransferase activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016746 | molecular_function | acyltransferase activity |
| F | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE COA A 301 |
| Chain | Residue |
| A | LEU2 |
| A | GLY48 |
| A | GLY111 |
| A | MET112 |
| A | GLY113 |
| A | GLN114 |
| A | ALA176 |
| A | SER180 |
| A | HOH302 |
| A | ILE5 |
| A | SER37 |
| A | SER38 |
| A | LEU39 |
| A | SER40 |
| A | GLY43 |
| A | TRP44 |
| A | VAL45 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE COA B 302 |
| Chain | Residue |
| B | SER37 |
| B | SER38 |
| B | LEU39 |
| B | SER40 |
| B | GLY43 |
| B | TRP44 |
| B | VAL45 |
| B | GLY48 |
| B | GLY111 |
| B | MET112 |
| B | GLY113 |
| B | GLN114 |
| B | ALA176 |
| B | SER180 |
| B | HOH318 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE COA C 303 |
| Chain | Residue |
| C | LEU2 |
| C | SER37 |
| C | SER38 |
| C | LEU39 |
| C | SER40 |
| C | GLY43 |
| C | TRP44 |
| C | VAL45 |
| C | GLY48 |
| C | GLY111 |
| C | MET112 |
| C | GLY113 |
| C | GLN114 |
| C | ALA176 |
| C | SER180 |
| C | HOH304 |
| C | HOH309 |
| C | HOH316 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE COA D 304 |
| Chain | Residue |
| D | LEU2 |
| D | ILE5 |
| D | SER37 |
| D | SER38 |
| D | LEU39 |
| D | SER40 |
| D | GLY43 |
| D | TRP44 |
| D | VAL45 |
| D | GLY48 |
| D | MET112 |
| D | GLY113 |
| D | GLN114 |
| D | ALA176 |
| D | SER180 |
| D | HOH305 |
| D | HOH312 |
| D | HOH327 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE COA E 305 |
| Chain | Residue |
| E | SER37 |
| E | SER38 |
| E | LEU39 |
| E | SER40 |
| E | GLY43 |
| E | TRP44 |
| E | VAL45 |
| E | GLY48 |
| E | GLY111 |
| E | MET112 |
| E | GLY113 |
| E | GLN114 |
| E | ALA176 |
| E | SER180 |
| E | HOH306 |
| E | HOH308 |
| E | HOH313 |
| E | HOH327 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of yokD protein from Bacillus subtilis.","authoringGroup":["New York structural genomix research consortium (NYSGXRC)"]}}]} |
| Chain | Residue | Details |
