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Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase

Analyse Structural and theoretical studies suggest domain movement produces an active… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2TPT
Type: protein
Length: 440 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidine phosphorylase
EC: 2.4.2.4
UniProt: P07650
Ligands: SO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidine phosphorylase (EC 2.4.2.4)	protein	440	47% helix, 16% strand	P07650

Ligands and binding sites

SO4 · Sulfate 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	524	0.74	0.82	45	SO4
2	60	0.69	0.96	23	empty

Compared structures

2TPT · Structural and theoretical studies suggest domain movement produces an active… · the same entry in another collection · chain A against A, TM-score 1.00
P07650 · AlphaFold monomer V2.0 prediction for thymidine phosphorylase (P07650) · 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 P07650
Elsewhere: RCSB PDB 2TPT · PDBe 2TPT · UniProt P07650

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