Research workbench
Deletion of a buried salt-bridge in barnase
Analyse Deletion of a buried salt-bridge in barnase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B20
- Type
- protein
- Length
- 326 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (barnase)
- EC
- 3.1.27.3
- UniProt
- P00648
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Protein (barnase) (EC 3.1.27.3) | protein | 109 | 23% helix, 23% strand | P00648 |
| B | Protein (barnase) (EC 3.1.27.3) | protein | 108 | 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 722 | 0.69 | 0.76 | 72 | empty |
| 2 | 52 | 0.26 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 181 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 165 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 61 Ų buried · 0 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 P00648
- Elsewhere: RCSB PDB 1B20 · PDBe 1B20 · UniProt P00648
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