MolNFT v1 · #23090 · protein
The three-dimensional structure of tyrosine phenol-lyase
1TPL: “The three-dimensional structure of tyrosine phenol-lyase”. X-ray diffraction, 1 ligand (SO4), 12 pockets (best druggability 0.64). MolNFT v1 #23090 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1TPL
- Type
- protein
- Length
- 852 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
- P31012
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine phenol-lyase (EC 4.1.99.2) | protein | 426 | 43% helix, 16% strand | P31012 |
| B | Tyrosine phenol-lyase (EC 4.1.99.2) | protein | 426 | 43% helix, 18% strand | P31012 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 404 | 0.64 | 0.78 | 57 | empty |
| 2 | 460 | 0.62 | 0.76 | 61 | SO4 |
| 3 | 394 | 0.58 | 0.75 | 57 | empty |
| 4 | 178 | 0.52 | 0.78 | 28 | empty |
| 5 | 117 | 0.43 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1871 Ų buried · 32 hydrogen bonds · protein-protein
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 P31012
- Elsewhere: RCSB PDB 1TPL · PDBe 1TPL · UniProt P31012
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