MolNFT v1 · #47727 · protein

Crystal structure of a glycosyltransferase involved in the glycosylation of the major capsid of pbcv-1

2P73 · Putative glycosyltransferase (mannosyltransferase) involved…: “Crystal structure of a glycosyltransferase involved in the glycosylation of the major capsid of pbcv-1”. X-ray diffraction, 2 ligands (UDP, MN), 1 pocket (best…

PDB: 2P73
Type: protein
Length: 207 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glycosyltransferase (mannosyltransferase) involved in glycosylating the pbcv-1…
UniProt: Q89399
Ligands: UDP, MN
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative glycosyltransferase (mannosyltransferase) involved in glycosylating the pbcv-1 major capsid protein	protein	207	36% helix, 18% strand	Q89399

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · chains A
MN · Manganese (II) 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	295	0.62	0.80	36	UDP

Compared structures

2P73 · crystal structure of a glycosyltransferase involved in the glycosylation of the major… · 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 Q89399
Elsewhere: RCSB PDB 2P73 · PDBe 2P73 · UniProt Q89399

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