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T. maritima fdts with FAD, dump, and folinic acid

Analyse T. maritima fdts with FAD, dump, and folinic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GTA
Type: protein
Length: 215 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, FFO, CL
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase thyx (EC 2.1.1.148)	protein	215	52% helix, 17% strand	Q9WYT0

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A
FFO · N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid · 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	90	0.40	0.77	19	empty

Compared structures

4GTA · T. Maritima FDTS with FAD, dUMP, and Folinic Acid · 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 4GTA · PDBe 4GTA · UniProt Q9WYT0

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