MolNFT v1 · #118162 · protein

E. COLI 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with ampcpp and inhibitor at 1.40 ångström resolution

5ETN · 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine…: “E. COLI 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with ampcpp and inhibitor at 1.40…”. X-ray diffraction, 4 ligands (ATP, 5RX, CA), 1 pocket (best druggability…

PDB: 5ETN
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
EC: 2.7.6.3
UniProt: P26281
Ligands: ATP, 5RX, CA, NA
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3)	protein	159	30% helix, 27% strand	P26281

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
5RX · 2-azanyl-8-[(4-chlorophenyl)methylsulfanyl]-1,9-dihydropurin-6-one · ligand · chains A
CA · Calcium ion · metal · 4 copies · chains A
NA · Sodium ion · metal · chains A

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

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	304	0.62	0.79	40	CA, ATP, 5RX

Compared structures

5ETN · E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and… · 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 P26281
Elsewhere: RCSB PDB 5ETN · PDBe 5ETN · UniProt P26281

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