MolNFT v1 · #137109 · protein

Crystal structure of UTP-glucose-1-phosphate uridylyltransferase from burkholderia ambifaria in complex with UTP

5VE7 · UTP--glucose-1-phosphate uridylyltransferase: “Crystal structure of UTP-glucose-1-phosphate uridylyltransferase from burkholderia ambifaria in complex with…”. X-ray diffraction, 1 ligand (UTP), 3 pockets (best druggability 0.64).…

PDB: 5VE7
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: UTP--glucose-1-phosphate uridylyltransferase
EC: 2.7.7.9
UniProt: B1YNX3
Ligands: UTP
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9)	protein	282	41% helix, 25% strand	B1YNX3

Ligands and binding sites

UTP · Uridine 5'-triphosphate · ligand · chains A

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

Pockets

3 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	443	0.64	0.78	41	UTP
2	74	0.35	0.76	19	empty
3	55	0.30	0.76	12	empty

Compared structures

5VE7 · Crystal structure of UTP-glucose-1-phosphate uridylyltransferase from Burkholderia… · 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 B1YNX3
Elsewhere: RCSB PDB 5VE7 · PDBe 5VE7 · UniProt B1YNX3

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