Research workbench
Crystal structure of human RECQL5 helicase in complex with ADP/MG.
Analyse Crystal structure of human RECQL5 helicase in complex with ADP/MG. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LB3
- Type
- protein
- Length
- 878 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent DNA helicase Q5
- EC
- 3.6.4.12
- UniProt
- O94762
- Ligands
- ADP, ZN, MG
- Pockets
- 10 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | ATP-dependent DNA helicase Q5 (EC 3.6.4.12) | protein | 439 | 48% helix, 14% strand | O94762 |
| E | ATP-dependent DNA helicase Q5 (EC 3.6.4.12) | protein | 439 | 48% helix, 15% strand | O94762 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains B, E
- ZN · Zinc ion · metal · 2 copies · chains B, E
- MG · Magnesium ion · metal · 2 copies · chains B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 480 | 0.63 | 0.76 | 54 | empty |
| 2 | 434 | 0.62 | 0.77 | 69 | ADP, MG |
| 3 | 102 | 0.62 | 0.88 | 16 | empty |
| 4 | 118 | 0.51 | 0.81 | 15 | empty |
| 5 | 120 | 0.48 | 0.80 | 17 | empty |
Interfaces
1 interface between chains.
- B–E · 122 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5LB3 · Crystal structure of human RECQL5 helicase in complex with ADP/Mg. · the same entry in another collection · chain B against B, TM-score 1.00
- O94762 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase Q5 (O94762) · a predicted model of the same protein · chain B against A, TM-score 0.79
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 O94762
- Elsewhere: RCSB PDB 5LB3 · PDBe 5LB3 · UniProt O94762
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