Research workbench
Assembly chaperone of RPL4 (ACL4) (residues 28-338)
Analyse Assembly chaperone of RPL4 (ACL4) (residues 28-338) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YNV
- Type
- protein
- Length
- 566 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ACL4
- UniProt
- G0S0I4
- Pockets
- 5 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ACL4 | protein | 283 | 76% helix, 0% strand | G0S0I4 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.43 | 0.75 | 30 | empty |
| 2 | 131 | 0.40 | 0.74 | 27 | empty |
| 3 | 125 | 0.39 | 0.74 | 22 | empty |
| 4 | 115 | 0.38 | 0.74 | 19 | empty |
| 5 | 51 | 0.30 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 662 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4YNV · Assembly Chaperone of RpL4 (Acl4) (Residues 28-338) · the same entry in another collection · chain A against A, TM-score 1.00
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 G0S0I4
- Elsewhere: RCSB PDB 4YNV · PDBe 4YNV · UniProt G0S0I4
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