MolNFT v1 · #90317 · protein
Bombyx mori lipoprotein 7 isolated from its natural source at 1.33 a resolution
4EFP · 30KDA protein: “Bombyx mori lipoprotein 7 isolated from its natural source at 1.33 a resolution”. X-ray diffraction, 3 ligands (CD, K, SCN), 2 pockets (best druggability 0.68). MolNFT v1 #90317 on GenesisL1: 3D structure, binding…
- PDB
- 4EFP
- Type
- protein
- Length
- 470 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 30KDA protein
- UniProt
- E5EVW2
- Ligands
- CD, K, SCN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 30KDA protein | protein | 235 | 33% helix, 35% strand | E5EVW2 |
Ligands and binding sites
- CD · Cadmium ion · metal · 2 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
- SCN · Thiocyanate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- PGE · Triethylene glycol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains B
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 | 465 | 0.68 | 0.79 | 56 | EDO |
| 2 | 109 | 0.42 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 458 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 4EFP · Bombyx mori lipoprotein 7 isolated from its natural source at 1.33 A resolution · 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 E5EVW2
- Elsewhere: RCSB PDB 4EFP · PDBe 4EFP · UniProt E5EVW2
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