Research workbench
Crystal structure of the archaeal holliday junction resolvase hjc
Analyse Crystal structure of the archaeal holliday junction resolvase hjc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GEF
- Type
- protein
- Length
- 459 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Holliday junction resolvase
- UniProt
- Q9V301
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holliday junction resolvase | protein | 120 | 36% helix, 33% strand | Q9V301 |
| B | Holliday junction resolvase | protein | 116 | 30% helix, 34% strand | Q9V301 |
| D | Holliday junction resolvase | protein | 109 | 35% helix, 30% strand | Q9V301 |
| E | Holliday junction resolvase | protein | 114 | 30% helix, 34% strand | Q9V301 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B, D, E
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 | 1166 | 0.81 | 0.82 | 110 | SO4 |
| 2 | 120 | 0.46 | 0.79 | 26 | empty |
Interfaces
4 interfaces between chains.
- B–D · 870 Ų buried · 19 hydrogen bonds · protein-protein
- A–E · 868 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 663 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 648 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 1GEF · Crystal structure of the archaeal holliday junction resolvase HJC · the same entry in another collection · chain B against B, 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 Q9V301
- Elsewhere: RCSB PDB 1GEF · PDBe 1GEF · UniProt Q9V301
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