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Crystal structure of IGLON5 homodimer
Analyse Crystal structure of IGLON5 homodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DLE
- Type
- protein
- Length
- 542 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iglon family member 5
- UniProt
- A6NGN9
- Ligands
- NAG
- Pockets
- 4 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Iglon family member 5 | protein | 271 | 2% helix, 61% strand | A6NGN9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.40 | 0.81 | 15 | NAG |
| 2 | 62 | 0.36 | 0.78 | 21 | empty |
| 3 | 50 | 0.33 | 0.78 | 17 | NAG |
| 4 | 61 | 0.32 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 894 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 glycan, 6 disulfide (N-glycosylation, 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 A6NGN9
- Elsewhere: RCSB PDB 6DLE · PDBe 6DLE · UniProt A6NGN9
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