MolNFT v1 · #10168 · protein

Thymidylyltransferase complexed with ttp

1IIM · Glucose-1-phosphate thymidylyltransferase: “Thymidylyltransferase complexed with ttp”. X-ray diffraction, 1 ligand (TTP), 6 pockets (best druggability 0.75). MolNFT v1 #10168 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1IIM
Type: protein
Length: 578 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-1-phosphate thymidylyltransferase
EC: 2.7.7.24
UniProt: Q9F7K6
Ligands: TTP
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24)	protein	289	40% helix, 23% strand	Q9F7K6

Ligands and binding sites

TTP · Thymidine-5'-triphosphate · ligand · 4 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	508	0.75	0.83	53	TTP
2	424	0.74	0.84	43	TTP
3	275	0.60	0.79	35	TTP
4	193	0.56	0.80	21	TTP
5	61	0.37	0.79	15	empty

Interfaces

1 interface between chains.

A–B · 1555 Å² buried · 43 hydrogen bonds · protein-protein

Compared structures

1IIM · thymidylyltransferase complexed with TTP · 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 Q9F7K6
Elsewhere: RCSB PDB 1IIM · PDBe 1IIM · UniProt Q9F7K6

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