Research workbench
Crystal structure of the helicase domain of the GENE4 protein of bacteriophage T7
Analyse Crystal structure of the helicase domain of the GENE4 protein of bacteriophage… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CR0
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA PRIMASE/HELICASE
- EC
- 2.7.7.-
- UniProt
- P03692
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA PRIMASE/HELICASE (EC 2.7.7.-) | protein | 241 | 41% helix, 24% strand | P03692 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.53 | 0.79 | 29 | SO4 |
| 2 | 90 | 0.40 | 0.77 | 15 | empty |
Compared structures
- 1CR0 · Crystal structure of the helicase domain of the GENE4 protein of bacteriophage T7 · 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 P03692
- Elsewhere: RCSB PDB 1CR0 · PDBe 1CR0 · UniProt P03692
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