Research workbench
Mycobacterium tuberculosis folylpolyglutamate synthase complexed with ADP
Analyse Mycobacterium tuberculosis folylpolyglutamate synthase complexed with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VOS
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Folylpolyglutamate synthase protein folc
- EC
- 6.3.2.17
- UniProt
- O53174
- Ligands
- ADP, CO, MG
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folylpolyglutamate synthase protein folc (EC 6.3.2.17) | protein | 448 | 43% helix, 20% strand | O53174 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- CO · Cobalt (II) ion · metal · 4 copies · chains A
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 861 | 0.76 | 0.79 | 89 | ADP, MG, CO, GOL |
| 2 | 61 | 0.32 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 2VOS · Mycobacterium tuberculosis Folylpolyglutamate synthase complexed with ADP · 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 O53174
- Elsewhere: RCSB PDB 2VOS · PDBe 2VOS · UniProt O53174
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