Research workbench
Gabaculine complex of gsam
Analyse Gabaculine complex of gsam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FQ7
- Type
- protein
- Length
- 854 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate-1-semialdehyde 2,1-aminomutase
- EC
- 5.4.3.8
- UniProt
- P24630
- Ligands
- PXG
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) | protein | 427 | 43% helix, 16% strand | P24630 |
Ligands and binding sites
- PXG · 3-[O-phosphonopyridoxyl]--amino-benzoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.81 | 0.98 | 35 | PXG |
| 2 | 142 | 0.80 | 0.97 | 39 | PXG |
| 3 | 53 | 0.74 | 1.00 | 19 | empty |
| 4 | 51 | 0.72 | 0.99 | 18 | empty |
| 5 | 66 | 0.52 | 0.86 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 4755 Ų buried · 71 hydrogen bonds · protein-protein
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 P24630
- Elsewhere: RCSB PDB 3FQ7 · PDBe 3FQ7 · UniProt P24630
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