Research workbench
Crystal structure of FIP200 CLAW/P-optineurin lir complex
Analyse Crystal structure of FIP200 CLAW/P-optineurin lir complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CZM
- Type
- protein
- Length
- 206 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RB1-inducible coiled-coil protein 1; Optineurin lir
- UniProt
- Q8TDY2, Q96CV9
- Ligands
- CL
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RB1-inducible coiled-coil protein 1 | protein | 92 | 7% helix, 41% strand | Q8TDY2 |
| B | RB1-inducible coiled-coil protein 1 | protein | 94 | 6% helix, 40% strand | Q8TDY2 |
| C | Optineurin lir | protein | 9 | 0% helix, 33% strand | Q96CV9 |
| D | Optineurin lir | protein | 11 | 0% helix, 27% strand | Q96CV9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 87 | 0.38 | 0.75 | 12 | empty |
Interfaces
3 interfaces between chains.
- A–B · 751 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 552 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 527 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 7CZM · Crystal structure of FIP200 Claw/p-OPtineurin LIR complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q8TDY2 · AlphaFold monomer V2.0 prediction for RB1-inducible coiled-coil protein 1 (Q8TDY2) · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q96CV9 · AlphaFold monomer V2.0 prediction for optineurin (Q96CV9) · a predicted model of the same protein · chain C against A, TM-score 0.36
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 Q8TDY2
- Every structure of UniProt Q96CV9
- Elsewhere: RCSB PDB 7CZM · PDBe 7CZM · UniProt Q8TDY2 · UniProt Q96CV9
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