3DHI
Crystal Structure of Reduced Toluene 4-Monoxygenase Hydroxylase Complexed with Effector Protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0009056 | biological_process | catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018638 | molecular_function | toluene 4-monooxygenase activity |
A | 0042203 | biological_process | toluene catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0009056 | biological_process | catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
B | 0018638 | molecular_function | toluene 4-monooxygenase activity |
B | 0042203 | biological_process | toluene catabolic process |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0009056 | biological_process | catabolic process |
C | 0018638 | molecular_function | toluene 4-monooxygenase activity |
C | 0042203 | biological_process | toluene catabolic process |
E | 0004497 | molecular_function | monooxygenase activity |
E | 0009056 | biological_process | catabolic process |
E | 0042203 | biological_process | toluene catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FE A 600 |
Chain | Residue |
A | GLU104 |
A | GLU134 |
A | HIS137 |
A | GLU231 |
A | HOH501 |
A | FE601 |
A | ACT602 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE A 601 |
Chain | Residue |
A | GLU231 |
A | HIS234 |
A | FE600 |
A | ACT602 |
A | GLU134 |
A | GLU197 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACT A 602 |
Chain | Residue |
A | GLU104 |
A | GLU134 |
A | LEU192 |
A | PHE196 |
A | GLU197 |
A | GLU231 |
A | HOH501 |
A | FE600 |
A | FE601 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1PE A 603 |
Chain | Residue |
A | TRP167 |
A | GLY334 |
A | TRP338 |
A | THR341 |
A | THR392 |
A | LEU393 |
A | PRO394 |
A | PRO403 |
A | LEU464 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 1PE B 604 |
Chain | Residue |
B | GLN100 |
B | ARG104 |
B | GLN236 |
B | GLN237 |
B | TRP240 |
B | PRO248 |
B | ASP252 |
B | HOH792 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BTB C 605 |
Chain | Residue |
A | HOH732 |
C | VAL20 |
C | LYS33 |
C | TYR36 |
C | HIS37 |
C | HOH328 |
E | ASP93 |
E | HOH591 |
E | HOH676 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19033467, ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368, ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14, ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M, ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O, ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK, ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C, ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT, ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV |
Chain | Residue | Details |
A | GLU104 | |
A | GLU134 | |
A | HIS137 | |
A | GLU197 | |
A | GLU231 | |
A | HIS234 |