MolNFT v1 · #37781 · protein
G51S/S52T double mutant of L. casei fpgs
2GCB · Folylpolyglutamate synthase: “G51S/S52T double mutant of L. casei fpgs”. X-ray diffraction, 3 pockets (best druggability 0.72). MolNFT v1 #37781 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GCB
- Type
- protein
- Length
- 407 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Folylpolyglutamate synthase
- EC
- 6.3.2.17
- UniProt
- P15925
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folylpolyglutamate synthase (EC 6.3.2.17) | protein | 407 | 42% helix, 18% strand | P15925 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 643 | 0.72 | 0.79 | 66 | empty |
| 2 | 104 | 0.59 | 0.86 | 18 | empty |
| 3 | 56 | 0.34 | 0.78 | 15 | empty |
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 P15925
- Elsewhere: RCSB PDB 2GCB · PDBe 2GCB · UniProt P15925
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