Research workbench
The structure of tryptophan 7-halogenase (prna) suggests a mechanism for regioselective chlorination
Analyse The structure of tryptophan 7-halogenase (prna) suggests a mechanism for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AQJ
- Type
- protein
- Length
- 517 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan halogenase, prna
- UniProt
- P95480
- Ligands
- TRP, FAD, CL
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan halogenase, prna | protein | 517 | 42% helix, 21% strand | P95480 |
Ligands and binding sites
- TRP · Tryptophan · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.82 | 0.89 | 58 | CL, FAD |
| 2 | 68 | 0.75 | 0.99 | 22 | TRP |
| 3 | 208 | 0.53 | 0.77 | 33 | empty |
| 4 | 94 | 0.42 | 0.78 | 18 | empty |
| 5 | 117 | 0.42 | 0.77 | 23 | empty |
Compared structures
- 2AQJ · The structure of tryptophan 7-halogenase (PrnA) suggests a mechanism for regioselective… · the same entry in another collection · chain A against A, TM-score 1.00
- P95480 · AlphaFold monomer V2.0 prediction for flavin-dependent tryptophan halogenase prna (P95480) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P95480
- Elsewhere: RCSB PDB 2AQJ · PDBe 2AQJ · UniProt P95480
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