MolNFT v1 · #93131 · protein

T. maritima fdts with FAD, dump, and raltitrexed.

4GTB · Thymidylate synthase thyx: “T. maritima fdts with FAD, dump, and raltitrexed.”. X-ray diffraction, 4 ligands (FAD, UMP, D16), 1 pocket (best druggability 0.31). MolNFT v1 #93131 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4GTB
Type: protein
Length: 211 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase thyx
EC: 2.1.1.148
UniProt: Q9WYT0
Ligands: FAD, UMP, D16, CL
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase thyx (EC 2.1.1.148)	protein	211	51% helix, 18% strand	Q9WYT0

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A
D16 · Tomudex · ligand · chains A
CL · Chloride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.31	0.77	14	empty

Compared structures

4GTB · T. Maritima FDTS with FAD, dUMP, and Raltitrexed. · 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 Q9WYT0
Elsewhere: RCSB PDB 4GTB · PDBe 4GTB · UniProt Q9WYT0

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