Research workbench
Structure of human PIF1 helicase domain residues 200-641
Analyse Structure of human PIF1 helicase domain residues 200-641 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FHH
- Type
- protein
- Length
- 788 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent DNA helicase PIF1
- EC
- 3.6.4.12
- UniProt
- Q9H611
- Ligands
- ADP, ALF
- Pockets
- 13 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase PIF1 (EC 3.6.4.12) | protein | 395 | 33% helix, 13% strand | Q9H611 |
| B | ATP-dependent DNA helicase PIF1 (EC 3.6.4.12) | protein | 393 | 33% helix, 11% strand | Q9H611 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- ALF · Tetrafluoroaluminate ion · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.82 | 0.93 | 41 | empty |
| 2 | 308 | 0.76 | 0.88 | 53 | empty |
| 3 | 872 | 0.76 | 0.80 | 117 | empty |
| 4 | 543 | 0.71 | 0.80 | 77 | empty |
| 5 | 286 | 0.68 | 0.83 | 52 | empty |
Interfaces
1 interface between chains.
- A–B · 778 Ų buried · 12 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 Q9H611
- Elsewhere: RCSB PDB 5FHH · PDBe 5FHH · UniProt Q9H611
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