Research workbench
Crystal structure of M-sec
Analyse Crystal structure of M-sec in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B86
- Type
- protein
- Length
- 1,157 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor necrosis factor alpha-induced protein 2
- UniProt
- Q61333
- Pockets
- 9 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor necrosis factor alpha-induced protein 2 | protein | 579 | 71% helix, 1% strand | Q61333 |
| B | Tumor necrosis factor alpha-induced protein 2 | protein | 578 | 70% helix, 0% strand | Q61333 |
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.62 | 0.93 | 17 | empty |
| 2 | 130 | 0.47 | 0.78 | 14 | empty |
| 3 | 112 | 0.43 | 0.77 | 16 | empty |
| 4 | 64 | 0.34 | 0.77 | 12 | empty |
| 5 | 54 | 0.32 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 42 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 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 Q61333
- Elsewhere: RCSB PDB 5B86 · PDBe 5B86 · UniProt Q61333
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