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Crystal structure yoph complexed with inhibitor pvs

Analyse Crystal structure yoph complexed with inhibitor pvs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BLU
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase yoph
EC: 3.1.3.48
UniProt: P15273
Ligands: PVS
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase yoph (EC 3.1.3.48)	protein	282	38% helix, 21% strand	P15273

Ligands and binding sites

PVS · (ethenylsulfonyl)benzene · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	200	0.52	0.78	22	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

3BLU · crystal structure YopH complexed with inhibitor PVS · the same entry in another collection · chain A against A, TM-score 1.00
P15273 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase yoph (P15273) · 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 P15273
Elsewhere: RCSB PDB 3BLU · PDBe 3BLU · UniProt P15273

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