MolNFT v1 · #72903 · protein
Crystal structure of borrelia burgdorferi pur-alpha
3NM7 · Uncharacterized protein: “Crystal structure of borrelia burgdorferi pur-alpha”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.66). MolNFT v1 #72903 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3NM7
- Type
- protein
- Length
- 309 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- O51076
- Ligands
- MG
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 4 distinct chains · 28% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 84 | 25% helix, 42% strand | O51076 |
| B | Uncharacterized protein | protein | 74 | 30% helix, 45% strand | O51076 |
| C | Uncharacterized protein | protein | 75 | 27% helix, 47% strand | O51076 |
| D | Uncharacterized protein | protein | 76 | 29% helix, 46% strand | O51076 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.66 | 0.82 | 47 | empty |
| 2 | 85 | 0.32 | 0.74 | 15 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2076 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 2043 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 624 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 198 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 187 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3NM7 · Crystal Structure of Borrelia burgdorferi Pur-alpha · 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 O51076
- Elsewhere: RCSB PDB 3NM7 · PDBe 3NM7 · UniProt O51076
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