MolNFT v1 · #175416 · protein
Crystal structure of SLX1-SLX4
7CQ2 · Structure-specific endonuclease subunit SLX1: “Crystal structure of SLX1-SLX4”. X-ray diffraction, 1 ligand (ZN), 10 pockets (best druggability 0.56). MolNFT v1 #175416 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7CQ2
- Type
- protein
- Length
- 716 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Structure-specific endonuclease subunit SLX1; SLX4 isoform 1
- EC
- 3.1.-.-
- UniProt
- A6ZLG6, A0A6A5PU22
- Ligands
- ZN
- Pockets
- 10 · best druggability 0.56
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Structure-specific endonuclease subunit SLX1 (EC 3.1.-.-) | protein | 274 | 45% helix, 18% strand | A6ZLG6 |
| B | Structure-specific endonuclease subunit SLX1 (EC 3.1.-.-) | protein | 297 | 37% helix, 18% strand | A6ZLG6 |
| C | SLX4 isoform 1 | protein | 74 | 64% helix, 5% strand | A0A6A5PU22 |
| D | SLX4 isoform 1 | protein | 71 | 65% helix, 6% strand | A0A6A5PU22 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.56 | 0.77 | 44 | empty |
| 2 | 180 | 0.51 | 0.78 | 31 | empty |
| 3 | 132 | 0.49 | 0.79 | 20 | empty |
| 4 | 120 | 0.48 | 0.79 | 21 | empty |
| 5 | 148 | 0.44 | 0.75 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1347 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 1174 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1031 Ų buried · 4 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 A6ZLG6
- Every structure of UniProt A0A6A5PU22
- Elsewhere: RCSB PDB 7CQ2 · PDBe 7CQ2 · UniProt A6ZLG6 · UniProt A0A6A5PU22
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