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Unliganded B-specific-1,3-galactosyltransferase G176R mutant (abbb)

Analyse Unliganded B-specific-1,3-galactosyltransferase G176R mutant (abbb) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RIZ
Type: protein
Length: 284 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoprotein-fucosylgalactoside alpha- galactosyltransferase
EC: 2.4.1.37
UniProt: P16442
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoprotein-fucosylgalactoside alpha- galactosyltransferase (EC 2.4.1.37)	protein	284	34% helix, 19% strand	P16442

Ligands and binding sites

GOL · Glycerol · additive · 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	417	0.63	0.77	31	empty

Compared structures

2RIZ · Unliganded B-specific-1,3-galactosyltransferase G176R mutant (ABBB) · the same entry in another collection · chain A against A, TM-score 1.00
P16442 · AlphaFold monomer V2.0 prediction for histo-blood group abo system transferase (P16442) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P16442
Elsewhere: RCSB PDB 2RIZ · PDBe 2RIZ · UniProt P16442

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