MolNFT v1 · #62504 · protein

Crystal structure of human thymidyalte synthase M190K with loop 181- 197 stabilized in the inactive conformation

3EHI · Thymidylate synthase: “Crystal structure of human thymidyalte synthase M190K with loop 181- 197 stabilized in the inactive…”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.68). MolNFT v1 #62504 on GenesisL1: 3D…

PDB: 3EHI
Type: protein
Length: 273 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 0.68

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Thymidylate synthase (EC 2.1.1.45)	protein	273	33% helix, 24% strand	P04818

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains X
EDO · 1,2-ethanediol · additive · 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	569	0.68	0.77	51	SO4
2	76	0.32	0.74	16	empty
3	51	0.28	0.75	19	empty
4	61	0.26	0.72	13	empty

Modifications

Observed in the structure: 2 modified (artifact).

Compared structures

3EHI · Crystal Structure of Human Thymidyalte Synthase M190K with Loop 181-197 stabilized in the… · 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 3EHI · PDBe 3EHI · UniProt P04818

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