MolNFT v1 · #17617 · protein
Structure of the recq catalytic core bound to ATP-gamma-S
1OYY · ATP-dependent DNA helicase: “Structure of the recq catalytic core bound to ATP-gamma-S”. X-ray diffraction, 3 ligands (AGS, MN, ZN), 7 pockets (best druggability 0.75). MolNFT v1 #17617 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1OYY
- Type
- protein
- Length
- 512 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent DNA helicase
- EC
- 3.6.1.-
- UniProt
- P15043
- Ligands
- AGS, MN, ZN
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase (EC 3.6.1.-) | protein | 512 | 44% helix, 15% strand | P15043 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 990 | 0.75 | 0.78 | 76 | MN, AGS |
| 2 | 278 | 0.63 | 0.80 | 48 | empty |
| 3 | 92 | 0.44 | 0.79 | 17 | empty |
| 4 | 54 | 0.36 | 0.79 | 15 | empty |
| 5 | 82 | 0.36 | 0.76 | 14 | empty |
Compared structures
- 1OYY · Structure of the RecQ Catalytic Core bound to ATP-gamma-S · the same entry in another collection · chain A against A, TM-score 1.00
- P15043 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase recq (P15043) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P15043
- Elsewhere: RCSB PDB 1OYY · PDBe 1OYY · UniProt P15043
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