MolNFT v1 · #52905 · protein
Crystal structures of mutant E46Q of tryptophan 5- halogenase (pyrh)
2WES · Tryptophan 5-halogenase: “Crystal structures of mutant E46Q of tryptophan 5- halogenase (pyrh)”. X-ray diffraction, 2 ligands (FAD, CL), 20 pockets (best druggability 0.81). MolNFT v1 #52905 on GenesisL1: 3D structure, binding sites…
- PDB
- 2WES
- Type
- protein
- Length
- 1,984 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan 5-halogenase
- UniProt
- A4D0H5
- Ligands
- FAD, CL
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Tryptophan 5-halogenase | protein | 496 | 40% helix, 22% strand | A4D0H5 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 441 | 0.81 | 0.89 | 53 | FAD, CL |
| 2 | 441 | 0.81 | 0.88 | 58 | FAD, CL |
| 3 | 421 | 0.80 | 0.88 | 52 | FAD, CL |
| 4 | 422 | 0.80 | 0.88 | 56 | FAD, CL |
| 5 | 1081 | 0.73 | 0.76 | 95 | empty |
Interfaces
3 interfaces between chains.
- A–D · 1894 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 1875 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 493 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2WES · Crystal structures of mutant E46Q of tryptophan 5-halogenase (PyrH) · the same entry in another collection · chain A against A, TM-score 1.00
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 A4D0H5
- Elsewhere: RCSB PDB 2WES · PDBe 2WES · UniProt A4D0H5
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