Research workbench
RV3666C bound to tripeptide
Analyse RV3666C bound to tripeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JLS
- Type
- protein
- Length
- 500 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable periplasmic dipeptide-binding lipoprotein dppa; Peptide ser-val-ala
- UniProt
- I6X811
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable periplasmic dipeptide-binding lipoprotein dppa | protein | 497 | 36% helix, 22% strand | I6X811 |
| B | Peptide ser-val-ala | protein | 3 | 0% helix, 33% strand | — |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.82 | 0.96 | 36 | empty |
| 2 | 201 | 0.80 | 0.95 | 38 | empty |
| 3 | 212 | 0.56 | 0.79 | 27 | empty |
| 4 | 57 | 0.39 | 0.80 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 339 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 7JLS · RV3666c bound to tripeptide · 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 I6X811
- Elsewhere: RCSB PDB 7JLS · PDBe 7JLS · UniProt I6X811
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