Research workbench
Water-mediate interaction at aprotein-protein interface
Analyse Water-mediate interaction at aprotein-protein interface in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X1W
- Type
- protein
- Length
- 596 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease; Barstar
- EC
- 3.1.27.-
- UniProt
- P00648, P11540
- Pockets
- 7 · best druggability 0.58
Structure
x-ray diffraction · 5 distinct chains · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease (EC 3.1.27.-) | protein | 108 | 22% helix, 23% strand | P00648 |
| B | Ribonuclease (EC 3.1.27.-) | protein | 110 | 22% helix, 24% strand | P00648 |
| C | Ribonuclease (EC 3.1.27.-) | protein | 109 | 22% helix, 23% strand | P00648 |
| D, E | Barstar | protein | 90 | 50% helix, 19% strand | P11540 |
| F | Barstar | protein | 89 | 49% helix, 18% strand | P11540 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 355 | 0.58 | 0.76 | 46 | empty |
| 2 | 294 | 0.51 | 0.74 | 32 | empty |
| 3 | 162 | 0.43 | 0.74 | 23 | empty |
| 4 | 130 | 0.43 | 0.76 | 21 | empty |
| 5 | 103 | 0.41 | 0.77 | 24 | empty |
Interfaces
6 interfaces between chains.
- B–E · 841 Ų buried · 15 hydrogen bonds · protein-protein
- C–F · 821 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 815 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 282 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 191 Ų buried · 3 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
- Every structure of UniProt P11540
- Elsewhere: RCSB PDB 1X1W · PDBe 1X1W · UniProt P00648 · UniProt P11540
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