3K28
Crystal Structure of a glutamate-1-semialdehyde aminotransferase from Bacillus anthracis with bound Pyridoxal 5'Phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| A | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| B | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| C | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| C | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| D | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0033014 | biological_process | tetrapyrrole biosynthetic process |
| D | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 900 |
| Chain | Residue |
| A | SER117 |
| A | MSE243 |
| A | LYS268 |
| A | HOH436 |
| A | HOH641 |
| A | HOH1249 |
| B | THR300 |
| B | HOH469 |
| A | GLY118 |
| A | THR119 |
| A | TYR145 |
| A | HIS146 |
| A | GLY147 |
| A | GLU207 |
| A | ASP240 |
| A | VAL242 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 430 |
| Chain | Residue |
| A | ILE103 |
| A | VAL106 |
| A | PRO107 |
| A | ILE109 |
| A | HOH517 |
| A | HOH1265 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 431 |
| Chain | Residue |
| A | HOH1248 |
| A | HOH1264 |
| A | HOH1431 |
| A | HOH1432 |
| A | HOH1433 |
| A | HOH1434 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 432 |
| Chain | Residue |
| A | ASP370 |
| A | HOH505 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 900 |
| Chain | Residue |
| A | THR300 |
| A | HOH566 |
| B | SER117 |
| B | GLY118 |
| B | THR119 |
| B | TYR145 |
| B | HIS146 |
| B | GLY147 |
| B | GLU207 |
| B | ASP240 |
| B | VAL242 |
| B | MSE243 |
| B | LYS268 |
| B | HOH439 |
| B | HOH543 |
| B | HOH1240 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 430 |
| Chain | Residue |
| B | ILE103 |
| B | VAL106 |
| B | PRO107 |
| B | ILE109 |
| B | HOH507 |
| B | HOH1262 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 431 |
| Chain | Residue |
| B | HOH996 |
| B | HOH1239 |
| B | HOH1427 |
| B | HOH1429 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CA B 432 |
| Chain | Residue |
| B | SER24 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 433 |
| Chain | Residue |
| B | ALA183 |
| B | ASP370 |
| B | HOH486 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP C 900 |
| Chain | Residue |
| C | SER117 |
| C | GLY118 |
| C | THR119 |
| C | TYR145 |
| C | HIS146 |
| C | GLU207 |
| C | ASN212 |
| C | ASP240 |
| C | VAL242 |
| C | MSE243 |
| C | LYS268 |
| C | HOH444 |
| C | HOH527 |
| C | HOH569 |
| D | THR300 |
| D | HOH540 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 430 |
| Chain | Residue |
| C | ILE103 |
| C | VAL106 |
| C | PRO107 |
| C | ILE109 |
| C | HOH492 |
| C | HOH1026 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 431 |
| Chain | Residue |
| A | GLU195 |
| C | PHE194 |
| C | ASN233 |
| C | HOH433 |
| C | HOH849 |
| C | HOH857 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 432 |
| Chain | Residue |
| C | ASP370 |
| C | HOH454 |
| C | HOH812 |
| site_id | BC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP D 900 |
| Chain | Residue |
| D | ASP240 |
| D | VAL242 |
| D | MSE243 |
| D | LYS268 |
| D | HOH440 |
| D | HOH500 |
| D | HOH542 |
| D | HOH561 |
| C | THR300 |
| D | SER117 |
| D | GLY118 |
| D | THR119 |
| D | TYR145 |
| D | HIS146 |
| D | GLU207 |
| D | ASN212 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 430 |
| Chain | Residue |
| D | ILE103 |
| D | VAL106 |
| D | PRO107 |
| D | ILE109 |
| D | HOH471 |
| D | HOH543 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA D 431 |
| Chain | Residue |
| D | HOH1253 |
| D | HOH1261 |
| D | HOH1423 |
| D | HOH1424 |
| D | HOH1425 |
| D | HOH1426 |
| D | HOH1430 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA D 432 |
| Chain | Residue |
| C | SER24 |
| C | HOH1450 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 433 |
| Chain | Residue |
| D | ALA183 |
| D | ASP370 |
| D | HOH450 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 37 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVmt.GF.RvAyncgqgyygvtp....DLTclGKvigGG |
| Chain | Residue | Details |
| A | LEU237-GLY273 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00375","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
