Research workbench
Crystal structure of human ARS2 residues 171-270 + 408-763 (P65 form)
Analyse Crystal structure of human ARS2 residues 171-270 + 408-763 (P65 form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F8D
- Type
- protein
- Length
- 782 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serrate RNA effector molecule homolog
- UniProt
- Q9BXP5
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 3 distinct chains · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serrate RNA effector molecule homolog | protein | 96 | 79% helix, 1% strand | Q9BXP5 |
| C, D | Serrate RNA effector molecule homolog | protein | 296 | 45% helix, 12% strand | Q9BXP5 |
| B | Serrate RNA effector molecule homolog | protein | 94 | 80% helix, 1% strand | Q9BXP5 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.71 | 0.79 | 46 | empty |
| 2 | 674 | 0.69 | 0.77 | 46 | empty |
| 3 | 313 | 0.61 | 0.78 | 39 | empty |
| 4 | 185 | 0.51 | 0.78 | 28 | empty |
| 5 | 185 | 0.51 | 0.77 | 29 | empty |
Interfaces
4 interfaces between chains.
- B–D · 3071 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 3064 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 510 Ų buried · 2 hydrogen bonds · protein-protein
- C–B · 82 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6F8D · Crystal structure of Human ARS2 residues 171-270 + 408-763 (P65 form) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BXP5 · AlphaFold monomer V2.0 prediction for serrate RNA effector molecule homolog (Q9BXP5) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 Q9BXP5
- Elsewhere: RCSB PDB 6F8D · PDBe 6F8D · UniProt Q9BXP5
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