Research workbench
M248I mutant of gsam
Analyse M248I mutant of gsam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FQ8
- 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
- PMP
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) | protein | 427 | 41% helix, 17% strand | P24630 |
Ligands and binding sites
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.82 | 0.97 | 39 | PMP |
| 2 | 149 | 0.81 | 0.97 | 37 | PMP |
| 3 | 66 | 0.76 | 0.99 | 21 | empty |
| 4 | 65 | 0.75 | 0.99 | 22 | empty |
| 5 | 50 | 0.70 | 0.98 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 4685 Ų buried · 70 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 3FQ8 · PDBe 3FQ8 · UniProt P24630
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