Research workbench
Crystal structure of monobody CS1/SHP2 C-SH2 domain complex
Analyse Crystal structure of monobody CS1/SHP2 C-SH2 domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JEG
- Type
- protein
- Length
- 207 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 11; Monobody CS1
- UniProt
- Q06124
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 11 | protein | 114 | 18% helix, 31% strand | Q06124 |
| B | Monobody CS1 | protein | 93 | 0% helix, 53% strand | — |
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 | 65 | 0.62 | 0.91 | 18 | empty |
| 2 | 131 | 0.45 | 0.77 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1142 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4JEG · Crystal Structure of Monobody CS1/SHP2 C-SH2 Domain Complex · 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 Q06124
- Elsewhere: RCSB PDB 4JEG · PDBe 4JEG · UniProt Q06124
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