Research workbench
MBC/SHP1-C-SH2 complex
Analyse MBC/SHP1-C-SH2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SM5
- Type
- protein
- Length
- 197 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 6; Mbc (monobody targeting SHP1-C-SH2)
- EC
- 3.1.3.48
- UniProt
- P29350
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) | protein | 106 | 20% helix, 42% strand | P29350 |
| B | Mbc (monobody targeting SHP1-C-SH2) | protein | 91 | 0% helix, 57% strand | — |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.53 | 0.81 | 22 | empty |
| 2 | 119 | 0.52 | 0.81 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 900 Ų buried · 14 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 P29350
- Elsewhere: RCSB PDB 6SM5 · PDBe 6SM5 · UniProt P29350
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