Research workbench

T4 phage bgt-D100A mutant in complex with udp-glucose: form II

Analyse T4 phage bgt-D100A mutant in complex with udp-glucose: form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NZF
Type: protein
Length: 351 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA beta-glycosyltransferase
EC: 2.4.1.27
UniProt: P04547
Ligands: UPG, CL
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA beta-glycosyltransferase (EC 2.4.1.27)	protein	351	39% helix, 17% strand	P04547

Ligands and binding sites

UPG · Uridine-5'-diphosphate-glucose · ligand · chains A
CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 2 copies · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	404	0.77	0.86	38	UPG, GOL
2	182	0.54	0.79	25	empty
3	136	0.48	0.78	24	CL

Compared structures

1NZF · T4 phage BGT-D100A mutant in complex with UDP-glucose: Form II · 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 P04547
Elsewhere: RCSB PDB 1NZF · PDBe 1NZF · UniProt P04547

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