MolNFT v1 · #52062 · protein
Structure of the bifunctional leishmania major trypanothione synthetase-amidase
2VPS: “Structure of the bifunctional leishmania major trypanothione synthetase-amidase”. X-ray diffraction, 2 ligands (CL, BR), 10 pockets (best druggability 0.65). MolNFT v1 #52062 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2VPS
- Type
- protein
- Length
- 603 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypanothione synthetase
- EC
- 6.3.1.9
- UniProt
- Q711P7
- Ligands
- CL, BR
- Pockets
- 10 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypanothione synthetase (EC 6.3.1.9) | protein | 603 | 26% helix, 28% strand | Q711P7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 353 | 0.65 | 0.80 | 37 | CL |
| 2 | 176 | 0.57 | 0.81 | 26 | empty |
| 3 | 305 | 0.56 | 0.76 | 47 | BR |
| 4 | 145 | 0.53 | 0.80 | 38 | empty |
| 5 | 150 | 0.49 | 0.77 | 17 | empty |
Compared structures
- 2VPS · Structure Of The Bifunctional Leishmania Major Trypanothione Synthetase-Amidase · 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 Q711P7
- Elsewhere: RCSB PDB 2VPS · PDBe 2VPS · UniProt Q711P7
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