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A new glycosyltransferase (DUF1792) from streptococcus sanguinis

Analyse A new glycosyltransferase (DUF1792) from streptococcus sanguinis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5V4A
Type: protein
Length: 536 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyltransferase (DUF1792)
UniProt: A3CM53
Ligands: UDP
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glycosyltransferase (DUF1792)	protein	268	42% helix, 16% strand	A3CM53

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

6 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	349	0.77	0.88	51	UDP
2	322	0.74	0.86	50	UDP
3	171	0.46	0.75	21	empty
4	155	0.45	0.76	22	empty
5	75	0.38	0.78	15	empty

Interfaces

1 interface between chains.

A–B · 664 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5V4A · A New Glycosyltransferase (DUF1792) from Streptococcus sanguinis · 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 A3CM53
Elsewhere: RCSB PDB 5V4A · PDBe 5V4A · UniProt A3CM53

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