Research workbench
Crystal structure of bovine low molecular weight protein tyrosine phosphatase (lmptp) mutant (W49Y N50E) complexed with vanadate and uncompetitive inhibitor
Analyse Crystal structure of bovine low molecular weight protein tyrosine phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JNW
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Low molecular weight phosphotyrosine protein phosphatase
- EC
- 3.1.3.48
- UniProt
- P11064
- Ligands
- 6LJ, VO4
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Low molecular weight phosphotyrosine protein phosphatase (EC 3.1.3.48) | protein | 154 | 45% helix, 15% strand | P11064 |
Ligands and binding sites
- 6LJ · 2-(4-{[3-(piperidin-1-yl)propyl]amino}quinolin-2-yl)benzonitrile · ligand · chains A
- VO4 · Vanadate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5JNW · Crystal structure of bovine low molecular weight protein tyrosine phosphatase (LMPTP)… · the same entry in another collection · chain A against A, TM-score 1.00
- P11064 · AlphaFold monomer V2.0 prediction for low molecular weight phosphotyrosine protein… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P11064
- Elsewhere: RCSB PDB 5JNW · PDBe 5JNW · UniProt P11064
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