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Crystal structure of human fanconi-associated nuclease 1
Analyse Crystal structure of human fanconi-associated nuclease 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RY3
- Type
- protein
- Length
- 593 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fanconi-associated nuclease 1
- EC
- 3.1.21.-, 3.1.4.1
- UniProt
- Q9Y2M0
- Ligands
- PT
- Pockets
- 8 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fanconi-associated nuclease 1 (EC 3.1.21.-, 3.1.4.1) | protein | 593 | 58% helix, 7% strand | Q9Y2M0 |
Ligands and binding sites
- PT · Platinum (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 386 | 0.61 | 0.77 | 35 | empty |
| 2 | 57 | 0.60 | 0.92 | 20 | empty |
| 3 | 297 | 0.57 | 0.77 | 33 | empty |
| 4 | 166 | 0.44 | 0.75 | 28 | empty |
| 5 | 126 | 0.43 | 0.76 | 25 | empty |
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 Q9Y2M0
- Elsewhere: RCSB PDB 4RY3 · PDBe 4RY3 · UniProt Q9Y2M0
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