MolNFT v1 · #35085 · protein
Mutant human ribonuclease 1 (V52L, D53L, N56L, F59L)
2E0O: “Mutant human ribonuclease 1 (V52L, D53L, N56L, F59L)”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.26). MolNFT v1 #35085 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2E0O
- Type
- protein
- Length
- 251 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease
- EC
- 3.1.27.5
- UniProt
- P07998
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.26
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease (EC 3.1.27.5) | protein | 126 | 21% helix, 35% strand | P07998 |
| B | Ribonuclease (EC 3.1.27.5) | protein | 125 | 20% helix, 35% strand | P07998 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.26 | 0.74 | 18 | SO4 |
Interfaces
1 interface between chains.
- A–B · 421 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
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 P07998
- Elsewhere: RCSB PDB 2E0O · PDBe 2E0O · UniProt P07998
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.