MolNFT v1 · #23221 · protein
Tryptophan synthase (E.C.4.2.1.20) in the presence of cesium, room temperature
1TTP: “Tryptophan synthase (E.C.4.2.1.20) in the presence of cesium, room temperature”. X-ray diffraction, 2 ligands (PLP, CS), 8 pockets (best druggability 0.79). MolNFT v1 #23221 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1TTP
- Type
- protein
- Length
- 645 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan synthase
- EC
- 4.2.1.20
- UniProt
- P00929, P00933
- Ligands
- PLP, CS
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase (EC 4.2.1.20) | protein | 256 | 53% helix, 14% strand | P00929 |
| B | Tryptophan synthase (EC 4.2.1.20) | protein | 389 | 47% helix, 21% strand | P00933 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.79 | 0.85 | 82 | PLP |
| 2 | 289 | 0.65 | 0.81 | 41 | empty |
| 3 | 74 | 0.50 | 0.84 | 17 | empty |
| 4 | 63 | 0.47 | 0.84 | 19 | empty |
| 5 | 75 | 0.38 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1296 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1TTP · Tryptophan synthase (E.C.4.2.1.20) in the presence of cesium, room temperature · the same entry in another collection · chain A against A, TM-score 1.00
- P00929 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (P00929) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P00929
- Every structure of UniProt P00933
- Elsewhere: RCSB PDB 1TTP · PDBe 1TTP · UniProt P00929 · UniProt P00933
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