MolNFT v1 · #36218 · protein
Holo tyrosine phenol-lyase from citrobacter freundii at pH 8.0
2EZ1: “Holo tyrosine phenol-lyase from citrobacter freundii at pH 8.0”. X-ray diffraction, 1 ligand (K), 10 pockets (best druggability 0.73). MolNFT v1 #36218 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2EZ1
- Type
- protein
- Length
- 910 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
- 10 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tyrosine phenol-lyase (EC 4.1.99.2) | protein | 455 | 46% 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
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 641 | 0.73 | 0.80 | 62 | empty |
| 2 | 567 | 0.72 | 0.80 | 53 | empty |
| 3 | 507 | 0.70 | 0.80 | 47 | empty |
| 4 | 491 | 0.69 | 0.80 | 45 | empty |
| 5 | 151 | 0.50 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2498 Ų buried · 32 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 2EZ1 · PDBe 2EZ1 · UniProt P31013
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