MolNFT v1 · #125519 · protein
Crystal structure of human RECQL5 helicase apo form.
5LB8 · ATP-dependent DNA helicase Q5: “Crystal structure of human RECQL5 helicase apo form.”. X-ray diffraction, 1 ligand (ZN), 7 pockets (best druggability 0.86). MolNFT v1 #125519 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5LB8
- Type
- protein
- Length
- 853 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
- ZN
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase Q5 (EC 3.6.4.12) | protein | 427 | 47% helix, 15% strand | O94762 |
| D | ATP-dependent DNA helicase Q5 (EC 3.6.4.12) | protein | 426 | 48% helix, 15% strand | O94762 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 543 | 0.86 | 0.92 | 91 | empty |
| 2 | 259 | 0.82 | 0.94 | 67 | empty |
| 3 | 242 | 0.63 | 0.82 | 37 | empty |
| 4 | 203 | 0.58 | 0.80 | 29 | empty |
| 5 | 102 | 0.45 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–D · 1549 Ų buried · 21 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 O94762
- Elsewhere: RCSB PDB 5LB8 · PDBe 5LB8 · UniProt O94762
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.