7CU0
Crystal structure of Streptomyces albogriseolus flavin-dependent tryptophan 6-halogenase Thal in complex with tryptophan
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue TRP A 601 |
| Chain | Residue |
| A | PRO53 |
| A | PHE465 |
| A | TRP466 |
| A | SER470 |
| A | HOH859 |
| A | HOH918 |
| A | LYS79 |
| A | HIS110 |
| A | PRO111 |
| A | PHE112 |
| A | GLU358 |
| A | TYR454 |
| A | TYR455 |
| A | GLU461 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue TRP B 601 |
| Chain | Residue |
| B | PRO53 |
| B | HIS110 |
| B | PRO111 |
| B | PHE112 |
| B | GLU358 |
| B | TYR454 |
| B | TYR455 |
| B | GLU461 |
| B | PHE465 |
| B | TRP466 |
| B | SER470 |
| B | HOH738 |
| B | HOH780 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:30559288, ECO:0000305|PubMed:33465708 |
| Chain | Residue | Details |
| A | LYS79 | |
| B | LYS79 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31589794, ECO:0000269|PubMed:33465708, ECO:0007744|PDB:6SLS, ECO:0007744|PDB:6SLT, ECO:0007744|PDB:7CU1 |
| Chain | Residue | Details |
| A | GLY13 | |
| B | ALA16 | |
| B | ILE42 | |
| B | ILE45 | |
| B | ALA50 | |
| B | MET198 | |
| B | LEU349 | |
| B | ILE362 | |
| A | ALA16 | |
| A | ILE42 | |
| A | ILE45 | |
| A | ALA50 | |
| A | MET198 | |
| A | LEU349 | |
| A | ILE362 | |
| B | GLY13 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33465708, ECO:0007744|PDB:7CU1 |
| Chain | Residue | Details |
| A | THR15 | |
| B | THR15 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31589794, ECO:0007744|PDB:6SLS |
| Chain | Residue | Details |
| A | ALA39 | |
| B | ALA39 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31589794, ECO:0007744|PDB:6SLS, ECO:0007744|PDB:6SLT |
| Chain | Residue | Details |
| A | VAL47 | |
| B | VAL47 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30559288, ECO:0000269|PubMed:31589794, ECO:0000269|PubMed:33465708, ECO:0007744|PDB:6H44, ECO:0007744|PDB:6SLT, ECO:0007744|PDB:7CU0 |
| Chain | Residue | Details |
| A | PRO111 | |
| B | PHE465 | |
| A | TYR454 | |
| A | TYR455 | |
| A | GLU461 | |
| A | PHE465 | |
| B | PRO111 | |
| B | TYR454 | |
| B | TYR455 | |
| B | GLU461 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:E9P162 |
| Chain | Residue | Details |
| A | SER360 | |
| A | GLY361 | |
| B | SER360 | |
| B | GLY361 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Important for activity => ECO:0000250|UniProtKB:P95480 |
| Chain | Residue | Details |
| A | GLU358 | |
| B | GLU358 |
