Research workbench
The crystal structure of the C-terminal domain of T. thermophilus uvrd complexed with the N-terminal domain of uvrb
Analyse The crystal structure of the C-terminal domain of T. thermophilus uvrd… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EGT
- Type
- protein
- Length
- 912 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uvrabc system protein B; DNA helicase uvrd
- EC
- 3.6.4.12
- UniProt
- Q56243, O24736
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Uvrabc system protein B | protein | 409 | 44% helix, 20% strand | Q56243 |
| B, D | DNA helicase uvrd (EC 3.6.4.12) | protein | 47 | 9% helix, 57% strand | O24736 |
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 | 584 | 0.74 | 0.81 | 53 | empty |
| 2 | 549 | 0.73 | 0.81 | 51 | empty |
| 3 | 721 | 0.66 | 0.75 | 68 | empty |
| 4 | 519 | 0.62 | 0.75 | 52 | empty |
| 5 | 84 | 0.51 | 0.84 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–D · 611 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 605 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 415 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7EGT · The crystal structure of the C-terminal domain of T. thermophilus UvrD complexed with the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q56243 · AlphaFold monomer V2.0 prediction for uvrabc system protein B (Q56243) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q56243
- Every structure of UniProt O24736
- Elsewhere: RCSB PDB 7EGT · PDBe 7EGT · UniProt Q56243 · UniProt O24736
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