Research workbench
Structure of RLD2 brx domain bound to LZY3 ccl motif
Analyse Structure of RLD2 brx domain bound to LZY3 ccl motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L0W
- Type
- protein
- Length
- 154 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RLD2; NGR2
- UniProt
- F4K0X5, Q5XVG3
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | RLD2 | protein | 61 | 30% helix, 34% strand | F4K0X5 |
| B, D | NGR2 | protein | 16 | 0% helix, 50% strand | Q5XVG3 |
Ligands and binding sites
- FLC · Citrate anion · additive · 2 copies · chains A, C
- EDO · 1,2-ethanediol · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.29 | 0.75 | 16 | empty |
Interfaces
4 interfaces between chains.
- A–B · 770 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 768 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 443 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 35 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
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 F4K0X5
- Every structure of UniProt Q5XVG3
- Elsewhere: RCSB PDB 6L0W · PDBe 6L0W · UniProt F4K0X5 · UniProt Q5XVG3
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