MolNFT v1 · #75876 · protein

Crystal structure of the actinobacillus pleuropneumoniae HMW1C glycosyltransferase

3Q3E · HMW1C-like glycosyltransferase: “Crystal structure of the actinobacillus pleuropneumoniae HMW1C glycosyltransferase”. X-ray diffraction, 10 pockets (best druggability 0.77). MolNFT v1 #75876 on GenesisL1: 3D structure, binding sites…

PDB: 3Q3E
Type: protein
Length: 1,216 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HMW1C-like glycosyltransferase
UniProt: E0EAD4
Pockets: 10 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HMW1C-like glycosyltransferase	protein	620	49% helix, 11% strand	E0EAD4
B	HMW1C-like glycosyltransferase	protein	596	52% helix, 12% strand	E0EAD4

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	825	0.77	0.80	63	GOL
2	769	0.75	0.80	65	GOL
3	56	0.66	0.95	20	empty
4	58	0.63	0.92	25	empty
5	108	0.45	0.78	16	empty

Compared structures

3Q3E · Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase · 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 E0EAD4
Elsewhere: RCSB PDB 3Q3E · PDBe 3Q3E · UniProt E0EAD4

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