Research workbench
The structure of phosphotyrosine phosphatase 1B in complex with compound 2
Analyse The structure of phosphotyrosine phosphatase 1B in complex with compound 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FJN
- Type
- protein
- Length
- 578 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase, non-receptor type 1
- EC
- 3.1.3.48
- UniProt
- P18031
- Ligands
- 073, CL
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tyrosine-protein phosphatase, non-receptor type 1 (EC 3.1.3.48) | protein | 289 | 37% helix, 21% strand | P18031 |
Ligands and binding sites
- 073 · (4-{(2S,4E)-2-(1H-1,2,3-benzotriazol-1-yl)-2-[4-(methoxycarbonyl)phenyl]-5-phenylpent-4-enyl}phenyl)(difluoro)methylphosphonic acid · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.76 | 0.78 | 98 | CL, 073 |
| 2 | 78 | 0.50 | 0.83 | 16 | empty |
| 3 | 52 | 0.38 | 0.80 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 501 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2FJN · The structure of phosphotyrosine phosphatase 1B in complex with compound 2 · the same entry in another collection · chain B against B, 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 P18031
- Elsewhere: RCSB PDB 2FJN · PDBe 2FJN · UniProt P18031
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