MolNFT v1 · #153895 · protein
Crystal structure of HRECQ1_D2-zn-wh containing mutation on beta- hairpin
6JTZ · ATP-dependent DNA helicase Q1: “Crystal structure of HRECQ1_D2-zn-wh containing mutation on beta- hairpin”. X-ray diffraction, 1 ligand (ZN), 10 pockets (best druggability 0.83). MolNFT v1 #153895 on GenesisL1: 3D structure, binding…
- PDB
- 6JTZ
- Type
- protein
- Length
- 604 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent DNA helicase Q1
- EC
- 3.6.4.12
- UniProt
- P46063
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent DNA helicase Q1 (EC 3.6.4.12) | protein | 303 | 40% helix, 17% strand | P46063 |
| B | ATP-dependent DNA helicase Q1 (EC 3.6.4.12) | protein | 301 | 41% helix, 17% strand | P46063 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
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 | 246 | 0.83 | 0.95 | 41 | empty |
| 2 | 421 | 0.60 | 0.76 | 37 | empty |
| 3 | 418 | 0.60 | 0.76 | 41 | empty |
| 4 | 123 | 0.55 | 0.83 | 25 | empty |
| 5 | 163 | 0.47 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1656 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 6JTZ · Crystal Structure of hRecQ1_D2-Zn-WH containing mutation on beta-hairpin · the same entry in another collection · chain A against A, TM-score 1.00
- P46063 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase Q1 (P46063) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P46063
- Elsewhere: RCSB PDB 6JTZ · PDBe 6JTZ · UniProt P46063
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