MolNFT v1 · #36888 · protein
The structure of phosphotyrosine phosphatase 1B in complex with compound 2
2FJM · Tyrosine-protein phosphatase, non-receptor type 1: “The structure of phosphotyrosine phosphatase 1B in complex with compound 2”. X-ray diffraction, 3 ligands (073, MG, CL), 4 pockets (best druggability 0.73). MolNFT v1 #36888 on…
- PDB
- 2FJM
- Type
- protein
- Length
- 570 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, MG, CL
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tyrosine-protein phosphatase, non-receptor type 1 (EC 3.1.3.48) | protein | 285 | 36% helix, 20% 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
- MG · Magnesium ion · metal · chains 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
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 828 | 0.73 | 0.78 | 62 | CL, 073 |
| 2 | 250 | 0.54 | 0.77 | 36 | empty |
| 3 | 85 | 0.50 | 0.82 | 16 | empty |
| 4 | 71 | 0.41 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 514 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2FJM · The structure of phosphotyrosine phosphatase 1B in complex with compound 2 · 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 P18031
- Elsewhere: RCSB PDB 2FJM · PDBe 2FJM · UniProt P18031
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