Research workbench
Crystal structure of optn E50K mutant and TBK1 complex
Analyse Crystal structure of optn E50K mutant and TBK1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EOA
- Type
- protein
- Length
- 229 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Optineurin; SERINE/THREONINE-protein kinase TBK1
- EC
- 2.7.11.1
- UniProt
- Q96CV9, Q9UHD2
Structure
x-ray diffraction · 4 distinct chains · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Optineurin | protein | 72 | 86% helix, 0% strand | Q96CV9 |
| B | Optineurin | protein | 73 | 89% helix, 0% strand | Q96CV9 |
| C | SERINE/THREONINE-protein kinase TBK1 (EC 2.7.11.1) | protein | 43 | 81% helix, 0% strand | Q9UHD2 |
| D | SERINE/THREONINE-protein kinase TBK1 (EC 2.7.11.1) | protein | 41 | 85% helix, 0% strand | Q9UHD2 |
Interfaces
6 interfaces between chains.
- B–C · 1127 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 1038 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 1003 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 991 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 988 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5EOA · Crystal structure of OPTN E50K mutant and TBK1 complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q9UHD2 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase TBK1 (Q9UHD2) · a predicted model of the same protein · chain D against A, TM-score 0.87
- Q96CV9 · AlphaFold monomer V2.0 prediction for optineurin (Q96CV9) · a predicted model of the same protein · chain A against A, TM-score 0.85
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 Q96CV9
- Every structure of UniProt Q9UHD2
- Elsewhere: RCSB PDB 5EOA · PDBe 5EOA · UniProt Q96CV9 · UniProt Q9UHD2
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