Research workbench

TAU55 histidine phosphatase domain

Analyse TAU55 histidine phosphatase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YN0
Type: protein
Length: 248 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription factor tau 55 kda subunit
UniProt: Q12415
Ligands: PO4
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription factor tau 55 kda subunit	protein	248	33% helix, 14% strand	Q12415

Ligands and binding sites

PO4 · Phosphate ion · ion · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.43	0.76	17	empty
2	97	0.39	0.76	16	PO4

Compared structures

2YN0 · tau55 histidine phosphatase domain · the same entry in another collection · chain A against A, TM-score 1.00
Q12415 · AlphaFold monomer V2.0 prediction for transcription factor tau 55 kda subunit (Q12415) · 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 Q12415
Elsewhere: RCSB PDB 2YN0 · PDBe 2YN0 · UniProt Q12415

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