MolNFT v1 · #2271 · protein
Barnase mutant with ile 96 replaced by ala
1BRK: “Barnase mutant with ile 96 replaced by ala”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.57). MolNFT v1 #2271 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1BRK
- Type
- protein
- Length
- 323 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Barnase
- EC
- 3.1.27.-
- UniProt
- P00648
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Barnase (EC 3.1.27.-) | protein | 108 | 22% helix, 23% strand | P00648 |
| C | Barnase (EC 3.1.27.-) | protein | 107 | 22% helix, 23% strand | P00648 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.57 | 0.75 | 32 | empty |
Interfaces
2 interfaces between chains.
- B–C · 200 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 45 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1BRK · Barnase mutant with ile 96 replaced by ala · the same entry in another collection · chain A against A, TM-score 1.00
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 P00648
- Elsewhere: RCSB PDB 1BRK · PDBe 1BRK · UniProt P00648
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.