Research workbench
Crystal structure of heptp with a closed wpd loop and an ordered E- loop
Analyse Crystal structure of heptp with a closed wpd loop and an ordered E- loop in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O4S
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 7
- EC
- 3.1.3.48
- UniProt
- P35236
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48) | protein | 293 | 38% helix, 23% strand | P35236 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.52 | 0.83 | 25 | SO4 |
| 2 | 76 | 0.38 | 0.78 | 17 | empty |
| 3 | 53 | 0.27 | 0.75 | 18 | empty |
| 4 | 51 | 0.23 | 0.72 | 16 | SO4 |
Compared structures
- 3O4S · Crystal Structure of HePTP with a Closed WPD Loop and an Ordered E-Loop · the same entry in another collection · chain A against A, TM-score 1.00
- P35236 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 7… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P35236
- Elsewhere: RCSB PDB 3O4S · PDBe 3O4S · UniProt P35236
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