Research workbench
Crystal structure of reduced toluene 4-monoxygenase hydroxylase complexed with effector protein
Analyse Crystal structure of reduced toluene 4-monoxygenase hydroxylase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DHI
- Type
- protein
- Length
- 989 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Toluene 4-monooxygenase hydroxylase alpha subunit; Toluene 4-monooxygenase hydroxylase…
- EC
- 1.14.13.-
- UniProt
- Q6Q8Q7, Q6Q8Q3, Q00457, Q00459
- Ligands
- FE
- Pockets
- 13 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 60% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toluene 4-monooxygenase hydroxylase alpha subunit | protein | 498 | 66% helix, 4% strand | Q6Q8Q7 |
| B | Toluene 4-monooxygenase hydroxylase beta subunit | protein | 306 | 70% helix, 0% strand | Q6Q8Q3 |
| C | Toluene 4-monooxygenase hydroxylase gamma subunit (EC 1.14.13.-) | protein | 82 | 17% helix, 38% strand | Q00457 |
| E | Toluene-4-monooxygenase system effector protein (EC 1.14.13.-) | protein | 103 | 32% helix, 36% strand | Q00459 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains A
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.71 | 0.98 | 22 | empty |
| 2 | 51 | 0.70 | 0.98 | 19 | ACT |
| 3 | 157 | 0.68 | 0.87 | 30 | 1PE |
| 4 | 143 | 0.64 | 0.87 | 36 | empty |
| 5 | 318 | 0.61 | 0.78 | 39 | empty |
Interfaces
3 interfaces between chains.
- A–B · 4374 Ų buried · 66 hydrogen bonds · protein-protein
- A–E · 1858 Ų buried · 35 hydrogen bonds · protein-protein
- A–C · 1330 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 3DHI · Crystal Structure of Reduced Toluene 4-Monoxygenase Hydroxylase Complexed with Effector… · the same entry in another collection · chain A against A, TM-score 1.00
- Q00457 · AlphaFold monomer V2.0 prediction for toluene-4-monooxygenase system, hydroxylase… · a predicted model of the same protein · chain C against A, TM-score 0.99
- Q00459 · AlphaFold monomer V2.0 prediction for toluene-4-monooxygenase system, effector component… · a predicted model of the same protein · chain E against A, TM-score 0.92
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q6Q8Q7
- Every structure of UniProt Q6Q8Q3
- Every structure of UniProt Q00457
- Every structure of UniProt Q00459
- Elsewhere: RCSB PDB 3DHI · PDBe 3DHI · UniProt Q6Q8Q7 · UniProt Q6Q8Q3 · UniProt Q00457 · UniProt Q00459
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