Research workbench
Crystal structure of lactococcal oppa co-crystallized with neuropeptide S in an open conformation
Analyse Crystal structure of lactococcal oppa co-crystallized with neuropeptide S in an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DRK
- Type
- protein
- Length
- 564 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oligopeptide-binding protein oppa; Neuropeptide S
- UniProt
- A2RJ53
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oligopeptide-binding protein oppa | protein | 559 | 30% helix, 23% strand | A2RJ53 |
| B | Neuropeptide S | protein | 5 | 0% helix, 40% strand | — |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1020 | 0.80 | 0.82 | 84 | empty |
| 2 | 349 | 0.70 | 0.83 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 410 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3DRK · Crystal structure of Lactococcal OppA co-crystallized with Neuropeptide S in an open… · 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 A2RJ53
- Elsewhere: RCSB PDB 3DRK · PDBe 3DRK · UniProt A2RJ53
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