Research workbench
E.COLI folc in complex with dhpp and ADP
Analyse E.COLI folc in complex with dhpp and ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W78
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Folc bifunctional protein
- EC
- 6.3.2.12
- UniProt
- P08192
- Ligands
- PD8, ADP, MG, SO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folc bifunctional protein (EC 6.3.2.12) | protein | 414 | 42% helix, 18% strand | P08192 |
Ligands and binding sites
- PD8 · Phosphorylated dihydropteroate · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · 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 | 824 | 0.79 | 0.82 | 85 | PD8, MG, ADP |
| 2 | 85 | 0.47 | 0.82 | 19 | 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 P08192
- Elsewhere: RCSB PDB 1W78 · PDBe 1W78 · UniProt P08192
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