MolNFT v1 · #114343 · protein
Lnmx protein, a putative glcnac-pi de-N-acetylase from streptomyces atroolivaceus
5BMO · Putative uncharacterized protein lnmx: “Lnmx protein, a putative glcnac-pi de-N-acetylase from streptomyces atroolivaceus”. X-ray diffraction, 1 ligand (K), 4 pockets (best druggability 0.77). MolNFT v1 #114343 on GenesisL1: 3D…
- PDB
- 5BMO
- Type
- protein
- Length
- 723 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein lnmx
- UniProt
- Q8GGM8
- Ligands
- K
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein lnmx | protein | 240 | 43% helix, 17% strand | Q8GGM8 |
| B | Putative uncharacterized protein lnmx | protein | 241 | 44% helix, 16% strand | Q8GGM8 |
| C | Putative uncharacterized protein lnmx | protein | 242 | 43% helix, 17% strand | Q8GGM8 |
Ligands and binding sites
- K · Potassium ion · metal · 3 copies · chains A, B, C
- ACT · Acetate ion · additive · 3 copies · chains A, B, C
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 | 876 | 0.77 | 0.80 | 60 | empty |
| 2 | 676 | 0.71 | 0.78 | 61 | K, ACT |
| 3 | 681 | 0.69 | 0.77 | 63 | ACT |
| 4 | 616 | 0.68 | 0.77 | 62 | ACT |
Interfaces
3 interfaces between chains.
- B–C · 583 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 573 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 565 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5BMO · LnmX protein, a putative GlcNAc-PI de-N-acetylase from Streptomyces atroolivaceus · 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 Q8GGM8
- Elsewhere: RCSB PDB 5BMO · PDBe 5BMO · UniProt Q8GGM8
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