Research workbench
Bacterial vitamin C transporter ULAA/SGAT in C2 form
Analyse Bacterial vitamin C transporter ULAA/SGAT in C2 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RP9
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ascorbate-specific permease iic component ulaa
- UniProt
- P39301
- Ligands
- BNG, ASC, TGL
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ascorbate-specific permease iic component ulaa | protein | 451 | 79% helix, 4% strand | P39301 |
Ligands and binding sites
- BNG · nonyl beta-D-glucopyranoside · ligand · 3 copies · chains A
- ASC · Ascorbic acid · ligand · chains A
- TGL · Tristearoylglycerol · ligand · chains A
- 1PE · Pentaethylene glycol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.66 | 0.84 | 21 | empty |
| 2 | 135 | 0.59 | 0.84 | 22 | ASC |
| 3 | 153 | 0.54 | 0.80 | 21 | BNG |
| 4 | 112 | 0.47 | 0.78 | 17 | empty |
| 5 | 74 | 0.42 | 0.79 | 15 | empty |
Compared structures
- 4RP9 · Bacterial vitamin C transporter UlaA/SgaT in C2 form · the same entry in another collection · chain A against A, TM-score 1.00
- P39301 · AlphaFold monomer V2.0 prediction for ascorbate-specific pts system eiic component… · 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 P39301
- Elsewhere: RCSB PDB 4RP9 · PDBe 4RP9 · UniProt P39301
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