Research workbench
Crystal structure of the hexadecameric form of RV3208A
Analyse Crystal structure of the hexadecameric form of RV3208A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RUR
- Type
- protein
- Length
- 257 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved protein of uncharacterized function, TB9.4
- UniProt
- A0A062W2V0
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 24% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conserved protein of uncharacterized function, TB9.4 | protein | 64 | 23% helix, 41% strand | A0A062W2V0 |
| B | Conserved protein of uncharacterized function, TB9.4 | protein | 63 | 24% helix, 41% strand | A0A062W2V0 |
| C, D | Conserved protein of uncharacterized function, TB9.4 | protein | 65 | 25% helix, 40% strand | A0A062W2V0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.77 | 0.92 | 45 | empty |
| 2 | 52 | 0.34 | 0.78 | 16 | empty |
| 3 | 50 | 0.34 | 0.79 | 13 | empty |
Interfaces
5 interfaces between chains.
- A–C · 926 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 917 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 518 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 444 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 141 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7RUR · Crystal structure of the hexadecameric form of Rv3208A · 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 A0A062W2V0
- Elsewhere: RCSB PDB 7RUR · PDBe 7RUR · UniProt A0A062W2V0
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