MolNFT v1 · #37222 · protein
Human alpha-phosphomannomutase 1 with D-mannose 1-phosphate and MG2+ cofactor bound
2FUE: “Human alpha-phosphomannomutase 1 with D-mannose 1-phosphate and MG2+ cofactor bound”. X-ray diffraction, 2 ligands (M1P, MG), 1 pocket (best druggability 0.60). MolNFT v1 #37222 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2FUE
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphomannomutase 1
- EC
- 5.4.2.8
- UniProt
- Q92871
- Ligands
- M1P, MG
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphomannomutase 1 (EC 5.4.2.8) | protein | 246 | 39% helix, 20% strand | Q92871 |
Ligands and binding sites
- M1P · 1-O-phosphono-alpha-D-mannopyranose · 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
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.60 | 0.78 | 43 | M1P, MG |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 2FUE · Human alpha-Phosphomannomutase 1 with D-mannose 1-phosphate and Mg2+ cofactor bound · the same entry in another collection · chain A against A, TM-score 1.00
- Q92871 · AlphaFold monomer V2.0 prediction for phosphomannomutase 1 (Q92871) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q92871
- Elsewhere: RCSB PDB 2FUE · PDBe 2FUE · UniProt Q92871
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