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Mutant human thymidylate synthase A191K crystallized in a sulfate-free condition

Analyse Mutant human thymidylate synthase A191K crystallized in a sulfate-free condition in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X4W
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: PO4
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase (EC 2.1.1.45)	protein	276	33% helix, 25% strand	P04818

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A

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	525	0.67	0.77	45	PO4
2	63	0.31	0.75	17	empty
3	50	0.28	0.75	15	empty
4	51	0.28	0.74	12	empty

Compared structures

5X4W · Mutant human thymidylate synthase A191K crystallized in a sulfate-free condition · the same entry in another collection · chain A against A, 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 5X4W · PDBe 5X4W · UniProt P04818

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