MolNFT v1 · #105493 · protein
Crystal structure of ABC transporter substrate-binding protein yeso from bacillus subtilis, target efi-510761, an open conformation
4R6K · Solute-binding protein: “Crystal structure of ABC transporter substrate-binding protein yeso from bacillus subtilis, target…”. X-ray diffraction, 1 ligand (NA), 3 pockets (best druggability 0.70). MolNFT v1 #105493 on GenesisL1: 3D…
- PDB
- 4R6K
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Solute-binding protein
- UniProt
- O31518
- Ligands
- NA
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Solute-binding protein | protein | 396 | 49% helix, 15% strand | O31518 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 512 | 0.70 | 0.80 | 67 | empty |
| 2 | 163 | 0.55 | 0.80 | 36 | empty |
| 3 | 69 | 0.36 | 0.77 | 12 | empty |
Compared structures
- 4R6K · Crystal structure of ABC transporter substrate-binding protein YesO from Bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- O31518 · AlphaFold monomer V2.0 prediction for putative ABC transporter substrate-binding protein… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O31518
- Elsewhere: RCSB PDB 4R6K · PDBe 4R6K · UniProt O31518
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