MolNFT v1 · #191072 · protein
Crystal structure of human RECQL5 helicase apo form in complex with engineered nanobody (gluebody) G4-043
7ZMS · ATP-dependent DNA helicase Q5: “Crystal structure of human RECQL5 helicase apo form in complex with engineered nanobody (gluebody) G4-043”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.69). MolNFT v1 #191072 on…
- PDB
- 7ZMS
- Type
- protein
- Length
- 561 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent DNA helicase Q5; Gluebody G4-043
- EC
- 3.6.4.12
- UniProt
- O94762
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase Q5 (EC 3.6.4.12) | protein | 437 | 50% helix, 15% strand | O94762 |
| K | Gluebody G4-043 | protein | 124 | 5% helix, 61% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 687 | 0.69 | 0.77 | 74 | empty |
| 2 | 78 | 0.37 | 0.76 | 17 | empty |
| 3 | 73 | 0.33 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–K · 770 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7ZMS · Crystal structure of human RECQL5 helicase APO form in complex with engineered nanobody… · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.72
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 7ZMS · PDBe 7ZMS · UniProt O94762
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