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Replacement of VAL3 in human thymidylate synthase affects its kinetic properties and intracellular stability

Analyse Replacement of VAL3 in human thymidylate synthase affects its kinetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GH2
Type: protein
Length: 276 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase
EC: 2.1.1.45
UniProt: P04818
Ligands: SO4
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Thymidylate synthase (EC 2.1.1.45)	protein	276	34% helix, 25% strand	P04818

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains X

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	251	0.51	0.75	36	SO4
2	114	0.37	0.74	17	empty
3	57	0.29	0.74	15	empty
4	53	0.28	0.75	17	empty

Modifications

Observed in the structure: 1 modified (artifact).

Compared structures

3GH2 · Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and… · the same entry in another collection · chain X against X, TM-score 1.00

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 P04818
Elsewhere: RCSB PDB 3GH2 · PDBe 3GH2 · UniProt P04818

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