MolNFT v1 · #6164 · protein

Crystal structure of escherichia COLI thymidylate synthase

1F4B: “Crystal structure of escherichia COLI thymidylate synthase”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.68). MolNFT v1 #6164 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1F4B
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
Ligands: SO4
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase (EC 2.1.1.45)	protein	264	35% helix, 26% strand	P0A884

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	567	0.68	0.77	49	empty
2	55	0.27	0.74	14	empty

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

1F4B · Crystal structure of escherichia COLI thymidylate synthase · 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 0.98

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 P0A884
Elsewhere: RCSB PDB 1F4B · PDBe 1F4B · UniProt P0A884

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