MolNFT v1 · #16978 · protein
Oxidation state of protein tyrosine phosphatase 1B
1OET · -tyrosine phosphatase, non-receptor type 1: “Oxidation state of protein tyrosine phosphatase 1B”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.44). MolNFT v1 #16978 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1OET
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- -tyrosine phosphatase, non-receptor type 1
- EC
- 3.1.3.48
- UniProt
- P18031
- Ligands
- MG
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | -tyrosine phosphatase, non-receptor type 1 (EC 3.1.3.48) | protein | 280 | 36% helix, 23% strand | P18031 |
Ligands and binding sites
- MG · Magnesium ion · metal · 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 | 123 | 0.44 | 0.77 | 22 | empty |
| 2 | 52 | 0.28 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 1OET · Oxidation state of protein tyrosine phosphatase 1B · 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 1OET · PDBe 1OET · UniProt P18031
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