MolNFT v1 · #16327 · protein

T4 phage bgt in complex with udp and a MN2+ ion at 1.8 a resolution

1NVK · DNA beta-glucosyltransferase: “T4 phage bgt in complex with udp and a MN2+ ion at 1.8 a resolution”. X-ray diffraction, 2 ligands (UDP, MN), 3 pockets (best druggability 0.76). MolNFT v1 #16327 on GenesisL1: 3D structure, binding…

PDB: 1NVK
Type: protein
Length: 351 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA beta-glucosyltransferase
EC: 2.4.1.27
UniProt: P04547
Ligands: UDP, MN
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA beta-glucosyltransferase (EC 2.4.1.27)	protein	351	40% helix, 18% strand	P04547

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · chains A
MN · Manganese (II) ion · metal · chains A
GOL · Glycerol · additive · 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	515	0.76	0.84	50	MN, UDP
2	126	0.45	0.77	21	GOL
3	75	0.40	0.78	16	empty

Compared structures

1NVK · T4 phage BGT in complex with UDP and a Mn2+ ion at 1.8 A resolution · 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 1NVK · PDBe 1NVK · UniProt P04547

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