Research workbench
Structure of human SHP2 without N-SH2 domain
Analyse Structure of human SHP2 without N-SH2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CMQ
- Type
- protein
- Length
- 1,574 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 11
- EC
- 3.1.3.48
- UniProt
- Q06124
- Pockets
- 20 · best druggability 0.66
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) | protein | 400 | 32% helix, 24% strand | Q06124 |
| B | Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) | protein | 394 | 33% helix, 23% strand | Q06124 |
| C | Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) | protein | 388 | 33% helix, 20% strand | Q06124 |
| D | Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) | protein | 392 | 32% helix, 26% strand | Q06124 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.66 | 0.96 | 21 | empty |
| 2 | 473 | 0.66 | 0.78 | 65 | empty |
| 3 | 260 | 0.58 | 0.79 | 48 | empty |
| 4 | 370 | 0.58 | 0.75 | 48 | empty |
| 5 | 272 | 0.55 | 0.76 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 741 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 735 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 599 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6CMQ · Structure of human SHP2 without N-SH2 domain · 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 6CMQ · PDBe 6CMQ · UniProt Q06124
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