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NMR structure of the mouse thiamine triphosphatase

Analyse NMR structure of the mouse thiamine triphosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JMU
Type: protein
Length: 224 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thiamine-triphosphatase
EC: 3.6.1.28
UniProt: Q8JZL3
Pockets: 1 · best druggability 0.55

Structure

solution nmr · 1 distinct chain · 31% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thiamine-triphosphatase (EC 3.6.1.28)	protein	224	31% helix, 33% strand	Q8JZL3

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	263	0.55	0.77	35	empty

Compared structures

2JMU · NMR structure of the mouse thiamine triphosphatase · the same entry in another collection · chain A against A, TM-score 1.00
Q8JZL3 · AlphaFold monomer V2.0 prediction for thiamine-triphosphatase (Q8JZL3) · a predicted model of the same protein · chain A against A, TM-score 0.52

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 Q8JZL3
Elsewhere: RCSB PDB 2JMU · PDBe 2JMU · UniProt Q8JZL3

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