3P1T
Crystal structure of a putative aminotransferase (BPSL1724) from Burkholderia pseudomallei K96243 at 2.60 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004400 | molecular_function | histidinol-phosphate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 338 |
| Chain | Residue |
| A | ARG258 |
| A | ARG265 |
| A | SER273 |
| A | EDO346 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TLA A 343 |
| Chain | Residue |
| A | PHE306 |
| A | ARG313 |
| A | HOH897 |
| A | HOH908 |
| B | TYR47 |
| A | PHE22 |
| A | ASN145 |
| A | TYR172 |
| A | LYS197 |
| A | LYS301 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 346 |
| Chain | Residue |
| A | ARG257 |
| A | ARG258 |
| A | SER274 |
| A | SO4338 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 349 |
| Chain | Residue |
| A | ASN69 |
| A | SER213 |
| A | GLU214 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 350 |
| Chain | Residue |
| A | ALA285 |
| A | GLU287 |
| A | ARG288 |
| A | HOH677 |
| A | HOH829 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 339 |
| Chain | Residue |
| B | ARG258 |
| B | ARG265 |
| B | SER273 |
| B | TLA342 |
| B | HOH916 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 340 |
| Chain | Residue |
| B | ASN145 |
| B | LYS301 |
| B | ARG313 |
| B | HOH909 |
| B | HOH911 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TLA B 342 |
| Chain | Residue |
| B | ARG257 |
| B | ARG258 |
| B | ALA261 |
| B | SER273 |
| B | SER274 |
| B | GLU275 |
| B | SO4339 |
| B | HOH916 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 347 |
| Chain | Residue |
| B | ASN283 |
| B | GLY286 |
| B | ASP302 |
| B | HIS309 |
| B | HIS310 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 351 |
| Chain | Residue |
| A | GLU115 |
| B | SER64 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 353 |
| Chain | Residue |
| B | ILE76 |
| B | PHE99 |
| B | ASN145 |
| B | ASP169 |
| B | THR171 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 356 |
| Chain | Residue |
| B | ALA285 |
| B | GLU287 |
| B | ARG288 |
| B | ARG291 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TLA C 344 |
| Chain | Residue |
| C | PHE22 |
| C | ASN145 |
| C | LYS197 |
| C | ARG205 |
| C | LYS301 |
| C | PHE306 |
| C | ARG313 |
| C | HOH913 |
| C | HOH915 |
| D | TYR47 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TLA C 345 |
| Chain | Residue |
| C | ARG257 |
| C | ARG258 |
| C | ARG265 |
| C | SER273 |
| C | SER274 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 348 |
| Chain | Residue |
| C | GLY286 |
| C | GLU287 |
| C | LEU290 |
| C | ASP302 |
| C | HIS309 |
| C | HIS310 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 352 |
| Chain | Residue |
| C | GLU282 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 357 |
| Chain | Residue |
| C | ALA285 |
| C | GLU287 |
| C | ARG288 |
| C | HIS310 |
| C | HOH870 |
| D | ARG54 |
| D | LYS58 |
| D | GLU237 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 337 |
| Chain | Residue |
| D | ARG258 |
| D | ARG265 |
| D | SER273 |
| D | TLA341 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TLA D 341 |
| Chain | Residue |
| D | SO4337 |
| D | ARG257 |
| D | ARG258 |
| D | SER273 |
| D | SER274 |
| D | GLU275 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 354 |
| Chain | Residue |
| D | PHE99 |
| D | ASN145 |
| D | ASP169 |
| D | THR171 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 358 |
| Chain | Residue |
| D | ALA285 |
| D | GLU287 |
| D | ARG288 |
| D | ARG291 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKsyGLaGLRLG |
| Chain | Residue | Details |
| A | SER194-GLY207 |
