Research workbench
Crystal structure of the mouse KIRREL3 D1 homodimer
Analyse Crystal structure of the mouse KIRREL3 D1 homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LU6
- Type
- protein
- Length
- 804 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kin of irre-like protein 3
- UniProt
- Q8BR86
- Ligands
- NA
- Pockets
- 7 · best druggability 0.54
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Kin of irre-like protein 3 | protein | 102 | 6% helix, 41% strand | Q8BR86 |
| B | Kin of irre-like protein 3 | protein | 101 | 6% helix, 42% strand | Q8BR86 |
| D, E, F, G | Kin of irre-like protein 3 | protein | 100 | 6% helix, 42% strand | Q8BR86 |
| H | Kin of irre-like protein 3 | protein | 99 | 6% helix, 40% strand | Q8BR86 |
Ligands and binding sites
- NA · Sodium ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.54 | 0.87 | 22 | empty |
| 2 | 65 | 0.41 | 0.80 | 20 | empty |
| 3 | 68 | 0.41 | 0.80 | 16 | empty |
| 4 | 53 | 0.40 | 0.81 | 17 | empty |
| 5 | 55 | 0.36 | 0.79 | 16 | empty |
Interfaces
7 interfaces between chains.
- F–G · 745 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 722 Ų buried · 6 hydrogen bonds · protein-protein
- B–E · 701 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 699 Ų buried · 6 hydrogen bonds · protein-protein
- G–H · 670 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 Q8BR86
- Elsewhere: RCSB PDB 7LU6 · PDBe 7LU6 · UniProt Q8BR86
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