Research workbench
Crystal structure of mutant ig-like domain
Analyse Crystal structure of mutant ig-like domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UD8
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triggering receptor expressed on myeloid cells 2
- UniProt
- Q9NZC2
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triggering receptor expressed on myeloid cells 2 | protein | 106 | 8% helix, 55% strand | Q9NZC2 |
| B | Triggering receptor expressed on myeloid cells 2 | protein | 104 | 3% helix, 57% strand | Q9NZC2 |
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 | 63 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 331 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 Q9NZC2
- Elsewhere: RCSB PDB 5UD8 · PDBe 5UD8 · UniProt Q9NZC2
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