MolNFT v1 · #150794 · protein
Proteus mirabilis N-acetylneuraminate lyase
6H4E · Putative N-acetylneuraminate lyase: “Proteus mirabilis N-acetylneuraminate lyase”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.65). MolNFT v1 #150794 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6H4E
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative N-acetylneuraminate lyase
- UniProt
- B4EZY4
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative N-acetylneuraminate lyase | protein | 295 | 52% helix, 14% strand | B4EZY4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.65 | 0.78 | 52 | SO4 |
| 2 | 444 | 0.65 | 0.77 | 46 | empty |
| 3 | 404 | 0.64 | 0.78 | 73 | empty |
Interfaces
1 interface between chains.
- A–B · 972 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6H4E · Proteus mirabilis N-acetylneuraminate lyase · the same entry in another collection · chain A against A, TM-score 1.00
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 B4EZY4
- Elsewhere: RCSB PDB 6H4E · PDBe 6H4E · UniProt B4EZY4
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