MolNFT v1 · #103831 · protein

Crystal structure of C.ELEGANS thymidylate synthase in complex with an inhibitor N(4)OHDCMP

4PSG: “Crystal structure of C.ELEGANS thymidylate synthase in complex with an inhibitor N(4)OHDCMP”. X-ray diffraction, 1 ligand (NOH), 9 pockets (best druggability 0.62). MolNFT v1 #103831 on GenesisL1: 3D structure, binding sites and…

PDB: 4PSG
Type: protein
Length: 578 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase
EC: 2.1.1.45
UniProt: Q9Y052
Ligands: NOH
Pockets: 9 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thymidylate synthase (EC 2.1.1.45)	protein	289	34% helix, 22% strand	Q9Y052

Ligands and binding sites

NOH · 2'-deoxy-N-hydroxycytidine 5'-(dihydrogen phosphate) · ligand · 2 copies · chains A, B

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

Pockets

9 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	371	0.62	0.78	25	NOH
2	403	0.62	0.77	33	NOH
3	125	0.44	0.77	21	empty
4	101	0.41	0.78	21	empty
5	88	0.41	0.78	17	empty

Interfaces

1 interface between chains.

A–B · 1926 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

4PSG · Crystal Structure of C.elegans Thymidylate Synthase in complex with an inhibitor… · 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 Q9Y052
Elsewhere: RCSB PDB 4PSG · PDBe 4PSG · UniProt Q9Y052

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.