Research workbench
Crystal structure of the helicase domain of the gene 4 protein of bacteriophage T7: complex with dtdp
Analyse Crystal structure of the helicase domain of the gene 4 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
- 1CR4
- Type
- protein
- Length
- 243 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
- TYD, SO4
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA PRIMASE/HELICASE (EC 2.7.7.-) | protein | 243 | 40% helix, 24% strand | P03692 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.47 | 0.78 | 25 | SO4, TYD |
| 2 | 65 | 0.44 | 0.81 | 21 | empty |
| 3 | 85 | 0.40 | 0.78 | 15 | empty |
Compared structures
- 1CR4 · Crystal structure of the helicase domain of the gene 4 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 1CR4 · PDBe 1CR4 · UniProt P03692
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