MolNFT v1 · #6531 · protein

Crystal structure of the apo-thymidylate synthase R166Q mutant

1FFL: “Crystal structure of the apo-thymidylate synthase R166Q mutant”. X-ray diffraction, 1 pocket (best druggability 0.67). MolNFT v1 #6531 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1FFL
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase
EC: 2.1.1.45
UniProt: P0A884
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase (EC 2.1.1.45)	protein	264	33% helix, 27% strand	P0A884

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	547	0.67	0.77	48	empty

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

1FFL · Crystal structure of the apo-thymidylate synthase R166Q mutant · the same entry in another collection · chain A against A, TM-score 1.00
P0A884 · AlphaFold monomer V2.0 prediction for thymidylate synthase (P0A884) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P0A884
Elsewhere: RCSB PDB 1FFL · PDBe 1FFL · UniProt P0A884

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