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NMR structure of the 140-315 fragment of the N-acetylglucosamine-1- phosphate transferase, alpha and beta subunits

Analyse NMR structure of the 140-315 fragment of the N-acetylglucosamine-1- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N6D
Type: protein
Length: 172 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylglucosamine-1-phosphotransferase subunits ALPHA/BETA
UniProt: Q3T906
Pockets: 3 · best druggability 0.73

Structure

solution nmr · 1 distinct chain · 16% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylglucosamine-1-phosphotransferase subunits ALPHA/BETA	protein	172	16% helix, 27% strand	Q3T906

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	233	0.73	0.88	32	empty
2	68	0.45	0.82	21	empty
3	84	0.39	0.77	19	empty

Compared structures

2N6D · NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphate transferase… · the same entry in another collection · chain A against A, TM-score 1.00
Q3T906 · AlphaFold monomer V2.0 prediction for N-acetylglucosamine-1-phosphotransferase subunits… · a predicted model of the same protein · chain A against A, TM-score 0.62

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 Q3T906
Elsewhere: RCSB PDB 2N6D · PDBe 2N6D · UniProt Q3T906

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