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Co-crystal structure of lmw-ptp in complex with 2-oxo-1-phenyl-2- (PHENYLAMINO)ETHANESULFONIC acid
Analyse Co-crystal structure of lmw-ptp in complex with 2-oxo-1-phenyl-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KQL
- 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, 3.1.3.2
- UniProt
- P24666
- Ligands
- 6VY
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Low molecular weight phosphotyrosine protein phosphatase (EC 3.1.3.48, 3.1.3.2) | protein | 154 | 44% helix, 15% strand | P24666 |
Ligands and binding sites
- 6VY · (1~{S})-2-oxidanylidene-1-phenyl-2-phenylazanyl-ethanesulfonic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.48 | 0.83 | 16 | 6VY |
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 P24666
- Elsewhere: RCSB PDB 5KQL · PDBe 5KQL · UniProt P24666
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