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Crystal structure of a trap periplasmic solute binding protein from anaerococcus prevotii dsm 20548 (APRE_1383), target efi-510023, with bound ALPHA/BETA D-glucuronate
Analyse Crystal structure of a trap periplasmic solute binding protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N91
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trap dicarboxylate transporter, dctp subunit
- UniProt
- C7RDZ3
- Ligands
- GCU, BDP, CL
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trap dicarboxylate transporter, dctp subunit | protein | 308 | 51% helix, 19% strand | C7RDZ3 |
Ligands and binding sites
- GCU · alpha-D-glucopyranuronic acid · sugar · chains A
- BDP · beta-D-glucopyranuronic acid · sugar · chains A
- CL · Chloride ion · ion · chains A
- PG4 · Tetraethylene glycol · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.69 | 0.92 | 30 | GCU, BDP, CL |
| 2 | 141 | 0.44 | 0.76 | 21 | empty |
| 3 | 136 | 0.43 | 0.76 | 25 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 4N91 · Crystal structure of a trap periplasmic solute binding protein from anaerococcus prevotii… · 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 C7RDZ3
- Elsewhere: RCSB PDB 4N91 · PDBe 4N91 · UniProt C7RDZ3
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