Research workbench
Crystal structure of arabidopsis thaliana profilin 2 complex with FORMIN1
Analyse Crystal structure of arabidopsis thaliana profilin 2 complex with FORMIN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IQJ
- Type
- protein
- Length
- 283 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Profilin-2; Formin-like protein 1
- UniProt
- Q42418, Q9SE97
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 3 distinct chains · 24% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Profilin-2 | protein | 131 | 28% helix, 31% strand | Q42418 |
| C | Formin-like protein 1 | protein | 12 | 0% helix, 0% strand | Q9SE97 |
| D | Formin-like protein 1 | protein | 9 | 0% helix, 0% strand | Q9SE97 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.58 | 0.85 | 22 | empty |
Interfaces
4 interfaces between chains.
- A–C · 546 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 437 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 284 Ų buried · 2 hydrogen bonds · protein-protein
- B–A · 202 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6IQJ · crystal structure of Arabidopsis thaliana Profilin 2 complex with formin1 · the same entry in another collection · chain B against B, TM-score 1.00
- Q42418 · AlphaFold monomer V2.0 prediction for profilin-2 (Q42418) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q9SE97 · AlphaFold monomer V2.0 prediction for formin-like protein 1 (Q9SE97) · a predicted model of the same protein · chain D against A, TM-score 0.58
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 Q42418
- Every structure of UniProt Q9SE97
- Elsewhere: RCSB PDB 6IQJ · PDBe 6IQJ · UniProt Q42418 · UniProt Q9SE97
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