Research workbench
Crystal structure of sulfolobus tokodaii PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE
Analyse Crystal structure of sulfolobus tokodaii PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F7L
- Type
- protein
- Length
- 910 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 455AA long hypothetical phospho-sugar mutase
- EC
- 5.4.2.8, 5.4.2.2
- UniProt
- Q976E4
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 455AA long hypothetical phospho-sugar mutase (EC 5.4.2.8, 5.4.2.2) | protein | 455 | 38% helix, 23% strand | Q976E4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 637 | 0.68 | 0.77 | 57 | SO4 |
| 2 | 493 | 0.63 | 0.76 | 50 | empty |
| 3 | 298 | 0.50 | 0.73 | 45 | empty |
| 4 | 87 | 0.50 | 0.83 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1024 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 2F7L · Crystal structure of Sulfolobus tokodaii phosphomannomutase/phosphoglucomutase · the same entry in another collection · chain A against A, TM-score 1.00
- Q976E4 · AlphaFold monomer V2.0 prediction for PHOSPHOGLUCOSAMINE/PHOSPHOGALACTOSAMINE mutase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q976E4
- Elsewhere: RCSB PDB 2F7L · PDBe 2F7L · UniProt Q976E4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.