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Crystal structure of helicase complex 1
Analyse Crystal structure of helicase complex 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WRX
- Type
- protein
- Length
- 1,699 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tm-1 protein; Replicase large subunit
- EC
- 2.1.1.-, 2.7.7.-, 2.7.7.48, 3.6.4.13
- UniProt
- A7M6E7, P03587
- Ligands
- AGS, CS, MG
- Pockets
- 17 · best druggability 0.63
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tm-1 protein | protein | 412 | 43% helix, 19% strand | A7M6E7 |
| B | Tm-1 protein | protein | 422 | 42% helix, 18% strand | A7M6E7 |
| C | Replicase large subunit (EC 2.1.1.-, 2.7.7.-, 2.7.7.48, 3.6.4.13) | protein | 434 | 33% helix, 22% strand | P03587 |
| D | Replicase large subunit (EC 2.1.1.-, 2.7.7.-, 2.7.7.48, 3.6.4.13) | protein | 431 | 33% helix, 23% strand | P03587 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 4 copies · chains A, C, B, D
- CS · Cesium ion · metal · 18 copies · chains A, B, D, C
- MG · Magnesium ion · metal · 3 copies · chains A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 458 | 0.63 | 0.76 | 44 | CS |
| 2 | 345 | 0.63 | 0.79 | 28 | empty |
| 3 | 152 | 0.62 | 0.85 | 28 | AGS, MG |
| 4 | 320 | 0.61 | 0.78 | 36 | empty |
| 5 | 133 | 0.56 | 0.83 | 25 | AGS |
Interfaces
3 interfaces between chains.
- A–B · 1791 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 1088 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 999 Ų buried · 17 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 A7M6E7
- Every structure of UniProt P03587
- Elsewhere: RCSB PDB 3WRX · PDBe 3WRX · UniProt A7M6E7 · UniProt P03587
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