Research workbench
Crystal structure of mle dsrbds in complex with ROX2 (R2H1)
Analyse Crystal structure of mle dsrbds in complex with ROX2 (R2H1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZTM
- Type
- protein + RNA
- Length
- 381 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dosage compensation regulator; Non-coding mRNA sequence ROX2
- EC
- 3.6.4.13
- UniProt
- P24785
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dosage compensation regulator (EC 3.6.4.13) | protein | 168 | 40% helix, 24% strand | P24785 |
| B | Dosage compensation regulator (EC 3.6.4.13) | protein | 164 | 41% helix, 23% strand | P24785 |
| C | Non-coding mRNA sequence ROX2 | rna | 49 | — | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1090 | 0.80 | 0.82 | 77 | empty |
| 2 | 233 | 0.62 | 0.82 | 29 | empty |
| 3 | 116 | 0.42 | 0.77 | 14 | empty |
| 4 | 84 | 0.34 | 0.76 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1420 Ų buried · 46 hydrogen bonds · protein-nucleic
- B–C · 1146 Ų buried · 18 hydrogen bonds · protein-nucleic
- A–B · 336 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 5ZTM · Crystal structure of MLE dsRBDs in complex with roX2 (R2H1) · the same entry in another collection · chain A against A, TM-score 1.00
- P24785 · AlphaFold monomer V2.0 prediction for dosage compensation regulator (P24785) · a predicted model of the same protein · chain A against A, TM-score 0.51
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 P24785
- Elsewhere: RCSB PDB 5ZTM · PDBe 5ZTM · UniProt P24785
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