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Structure of a dodecameric bacterial helicase
Analyse Structure of a dodecameric bacterial helicase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZC0
- Type
- protein
- Length
- 1,173 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Replicative DNA helicase
- EC
- 3.6.4.12
- UniProt
- O25916
- Ligands
- TBR
- Pockets
- 15 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 58% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replicative DNA helicase (EC 3.6.4.12) | protein | 445 | 54% helix, 14% strand | O25916 |
| B | Replicative DNA helicase (EC 3.6.4.12) | protein | 434 | 52% helix, 14% strand | O25916 |
| C | Replicative DNA helicase (EC 3.6.4.12) | protein | 148 | 71% helix, 0% strand | O25916 |
| D | Replicative DNA helicase (EC 3.6.4.12) | protein | 146 | 75% helix, 0% strand | O25916 |
Ligands and binding sites
- TBR · Hexatantalum dodecabromide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 692 | 0.76 | 0.82 | 76 | empty |
| 2 | 64 | 0.71 | 0.97 | 19 | empty |
| 3 | 539 | 0.71 | 0.80 | 54 | empty |
| 4 | 409 | 0.68 | 0.80 | 51 | empty |
| 5 | 57 | 0.58 | 0.90 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1552 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 919 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 221 Ų buried · 2 hydrogen bonds · protein-protein
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 O25916
- Elsewhere: RCSB PDB 4ZC0 · PDBe 4ZC0 · UniProt O25916
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