MolNFT v1 · #108009 · protein
Structural and biochemical characterization of the N- acetylmannosamine-6-phosphate 2-epimerase from clostridium perfringens
4UTU · N-acetylmannosamine-6-phosphate 2-epimerase: “Structural and biochemical characterization of the N- acetylmannosamine-6-phosphate 2-epimerase from…”. X-ray diffraction, 2 ligands (LRY, CL), 4 pockets (best druggability 0.61). MolNFT…
- PDB
- 4UTU
- Type
- protein
- Length
- 458 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylmannosamine-6-phosphate 2-epimerase
- EC
- 5.1.3.9
- UniProt
- Q8XNZ3
- Ligands
- LRY, CL
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-acetylmannosamine-6-phosphate 2-epimerase (EC 5.1.3.9) | protein | 229 | 40% helix, 16% strand | Q8XNZ3 |
Ligands and binding sites
- LRY · N-acetylmannosamine-6-phosphate · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.61 | 0.80 | 28 | LRY |
| 2 | 83 | 0.60 | 0.88 | 22 | empty |
| 3 | 231 | 0.59 | 0.80 | 24 | LRY |
| 4 | 57 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1638 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4UTU · Structural and biochemical characterization of the N- acetylmannosamine-6-phosphate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8XNZ3 · AlphaFold monomer V2.0 prediction for putative N-acetylmannosamine-6-phosphate… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q8XNZ3
- Elsewhere: RCSB PDB 4UTU · PDBe 4UTU · UniProt Q8XNZ3
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