MolNFT v1 · #22866 · protein

Crystal structure of thymidylate synthase from T4 phage

1TIS: “Crystal structure of thymidylate synthase from T4 phage”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.76). MolNFT v1 #22866 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1TIS
Type: protein
Length: 286 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase
EC: 2.1.1.45
UniProt: P00471
Ligands: PO4
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase (EC 2.1.1.45)	protein	286	37% helix, 20% strand	P00471

Ligands and binding sites

PO4 · Phosphate ion · ion · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	712	0.76	0.81	73	PO4
2	58	0.59	0.91	19	empty

Compared structures

1TIS · Crystal structure of thymidylate synthase from T4 phage · 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 P00471
Elsewhere: RCSB PDB 1TIS · PDBe 1TIS · UniProt P00471

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