Research workbench
X-ray structure of REB1-ter complex
Analyse X-ray structure of REB1-ter complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EYB
- Type
- protein + DNA
- Length
- 781 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein REB1; DNA (26-mer)
- UniProt
- Q9P6H9
- Pockets
- 15 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein REB1 | protein | 340 | 65% helix, 0% strand | Q9P6H9 |
| C, E | DNA (26-mer) | dna | 26 | — | — |
| D, F | DNA (26-mer) | dna | 26 | — | — |
| B | DNA-binding protein REB1 | protein | 337 | 65% helix, 0% strand | Q9P6H9 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.80 | 0.98 | 16 | empty |
| 2 | 93 | 0.77 | 0.98 | 15 | empty |
| 3 | 948 | 0.76 | 0.79 | 71 | empty |
| 4 | 1043 | 0.74 | 0.77 | 91 | empty |
| 5 | 287 | 0.55 | 0.76 | 35 | empty |
Interfaces
8 interfaces between chains.
- A–C · 1268 Ų buried · 29 hydrogen bonds · protein-nucleic
- B–E · 1234 Ų buried · 30 hydrogen bonds · protein-nucleic
- A–D · 1160 Ų buried · 10 hydrogen bonds · protein-nucleic
- C–D · 1124 Ų buried · 91 hydrogen bonds · nucleic-nucleic
- E–F · 1118 Ų buried · 93 hydrogen bonds · nucleic-nucleic
Compared structures
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 Q9P6H9
- Elsewhere: RCSB PDB 5EYB · PDBe 5EYB · UniProt Q9P6H9
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