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Flavin-dependent thymidylate synthase in complex with FAD and 2'- deoxyuridine-5'-monosulfate

Analyse Flavin-dependent thymidylate synthase in complex with FAD and 2'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IOR
Type: protein
Length: 216 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, DUS, RBF
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase thyx (EC 2.1.1.148)	protein	216	50% helix, 17% strand	Q9WYT0

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
DUS · 2'-deoxy-5'-O-sulfouridine · ligand · chains A
RBF · Riboflavin · ligand · 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	51	0.29	0.75	15	empty

Compared structures

5IOR · Flavin-dependent thymidylate synthase in complex with FAD and… · 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 5IOR · PDBe 5IOR · UniProt Q9WYT0

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