Research workbench
Crystal structure of rat protein tyrosine phosphatase eta catalytic domain
Analyse Crystal structure of rat protein tyrosine phosphatase eta catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I36
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vascular protein tyrosine phosphatase 1
- EC
- 3.1.3.48
- UniProt
- Q62884
- Ligands
- CL
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vascular protein tyrosine phosphatase 1 (EC 3.1.3.48) | protein | 286 | 38% helix, 21% strand | Q62884 |
Ligands and binding sites
- CL · Chloride ion · ion · 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 | 104 | 0.40 | 0.77 | 21 | empty |
| 2 | 50 | 0.27 | 0.74 | 15 | empty |
Compared structures
- 3I36 · Crystal Structure of Rat Protein Tyrosine Phosphatase eta Catalytic 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 Q62884
- Elsewhere: RCSB PDB 3I36 · PDBe 3I36 · UniProt Q62884
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