MolNFT v1 · #63422 · protein
W354F yersinia enterocolitica ptpase apo form
3F99 · Tyrosine-protein phosphatase yoph: “W354F yersinia enterocolitica ptpase apo form”. X-ray diffraction, 2 pockets (best druggability 0.47). MolNFT v1 #63422 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3F99
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase yoph
- EC
- 3.1.3.48
- UniProt
- P15273
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase yoph (EC 3.1.3.48) | protein | 282 | 38% helix, 21% strand | P15273 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.47 | 0.79 | 23 | empty |
| 2 | 144 | 0.44 | 0.76 | 23 | empty |
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 P15273
- Elsewhere: RCSB PDB 3F99 · PDBe 3F99 · UniProt P15273
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