MolNFT v1 · #146950 · protein
Citrobacter freundii tyrosine phenol-lyase F448A mutant
6DXV: “Citrobacter freundii tyrosine phenol-lyase F448A mutant”. X-ray diffraction, 1 ligand (K), 9 pockets (best druggability 0.76). MolNFT v1 #146950 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DXV
- Type
- protein
- Length
- 903 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine phenol-lyase
- EC
- 4.1.99.2
- UniProt
- P31013
- Ligands
- K
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine phenol-lyase (EC 4.1.99.2) | protein | 448 | 46% helix, 14% strand | P31013 |
| B | Tyrosine phenol-lyase (EC 4.1.99.2) | protein | 455 | 45% helix, 15% strand | P31013 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 493 | 0.76 | 0.84 | 65 | empty |
| 2 | 673 | 0.75 | 0.80 | 55 | empty |
| 3 | 526 | 0.73 | 0.81 | 50 | empty |
| 4 | 561 | 0.72 | 0.80 | 48 | empty |
| 5 | 235 | 0.61 | 0.80 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 2392 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
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 P31013
- Elsewhere: RCSB PDB 6DXV · PDBe 6DXV · UniProt P31013
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