Research workbench
Structural response to mutation at a protein-protein interface
Analyse Structural response to mutation at a protein-protein interface in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B2S
- Type
- protein
- Length
- 599 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (barnase); Protein (barstar)
- EC
- 3.1.27.3
- UniProt
- P00648, P11540
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.58
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Protein (barnase) (EC 3.1.27.3) | protein | 110 | 22% helix, 23% strand | P00648 |
| D, E | Protein (barstar) | protein | 90 | 49% helix, 18% strand | P11540 |
| F | Protein (barstar) | protein | 89 | 49% helix, 17% strand | P11540 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.58 | 0.75 | 46 | empty |
| 2 | 166 | 0.53 | 0.80 | 33 | empty |
| 3 | 143 | 0.52 | 0.80 | 34 | empty |
| 4 | 98 | 0.44 | 0.79 | 25 | empty |
| 5 | 64 | 0.37 | 0.79 | 15 | empty |
Interfaces
6 interfaces between chains.
- B–E · 817 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 785 Ų buried · 18 hydrogen bonds · protein-protein
- C–F · 779 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 303 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 274 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1B2S · Structural response to mutation at a protein-protein interface · the same entry in another collection · chain F against F, TM-score 1.00
- P00648 · AlphaFold monomer V2.0 prediction for ribonuclease (P00648) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P11540 · AlphaFold monomer V2.0 prediction for barstar (P11540) · a predicted model of the same protein · chain D against A, TM-score 0.98
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
- Every structure of UniProt P11540
- Elsewhere: RCSB PDB 1B2S · PDBe 1B2S · UniProt P00648 · UniProt P11540
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.