MolNFT v2 · #122752 · protein

Flavin-dependent thymidylate synthase in complex with FAD and deoxyuridine

5IOQ: “Flavin-dependent thymidylate synthase in complex with FAD and deoxyuridine”. X-ray diffraction at 1.93, 2 ligands (FAD, DUR). MolNFT v2 #122752 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5IOQ
Type: protein
Length: 851 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.93
Source: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
UniProt: Q9WYT0
Ligands: FAD, DUR

Structure

x-ray diffraction · resolution 1.93 · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	210	—	Q9WYT0
B	—	protein	210	—	Q9WYT0
C	—	protein	218	—	Q9WYT0
D	—	protein	213	—	Q9WYT0

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
DUR · 2'-deoxyuridine · ligand · 4 copies · chains A, B, C, D
PGE · Triethylene glycol · additive · 10 copies · chains A, B, D, C

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

Compared structures

5IOQ · Flavin-dependent thymidylate synthase in complex with FAD and deoxyuridine · the same entry in another collection · chain D against D, TM-score 1.00
Q9WYT0 · AlphaFold monomer V2.0 prediction for flavin-dependent thymidylate synthase (Q9WYT0) · a predicted model of the same protein · chain D against A, TM-score 0.98

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 5IOQ · PDBe 5IOQ · UniProt Q9WYT0

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