Research workbench
Fpgs-amppcp-folate complex
Analyse Fpgs-amppcp-folate complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JBW
- Type
- protein
- Length
- 410 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
- Ligands
- ACQ, TMF, MG
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folylpolyglutamate synthase (EC 6.3.2.17) | protein | 410 | 43% helix, 19% strand | P15925 |
Ligands and binding sites
- ACQ · Diphosphomethylphosphonic acid adenylate ester · ligand · chains A
- TMF · 5,10-methylene-6-hydrofolic acid · ligand · chains A
- MG · Magnesium ion · metal · 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 | 882 | 0.77 | 0.80 | 106 | MG, ACQ, TMF |
| 2 | 50 | 0.30 | 0.77 | 11 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
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 1JBW · PDBe 1JBW · UniProt P15925
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