MolNFT v1 · #93135 · protein
T. maritima fdts (H53A mutant) with FAD, dump and folate
4GTF · Thymidylate synthase thyx: “T. maritima fdts (H53A mutant) with FAD, dump and folate”. X-ray diffraction, 4 ligands (FAD, UMP, MEF). MolNFT v1 #93135 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4GTF
- Type
- protein
- Length
- 213 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, MEF, CL
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 | 213 | 52% helix, 17% strand | Q9WYT0 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A
- MEF · N-({4-[(6aR)-3-amino-1-oxo-1,2,5,6,6a,7-hexahydroimidazo[1,5-f]pteridin-8(9H)-yl]phenyl}carbonyl)-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.
Compared structures
- 4GTF · T. Maritima FDTS (H53A mutant) with FAD, dUMP and Folate · 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 4GTF · PDBe 4GTF · UniProt Q9WYT0
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