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Structural basis of specific recognition of non-reducing terminal N- acetylglucosamine by an agrocybe aegerita lection

Analyse Structural basis of specific recognition of non-reducing terminal N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TQM
Type: protein
Length: 402 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lectin 2
UniProt: H6CS64
Ligands: NAG, GAL
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lectin 2	protein	402	2% helix, 36% strand	H6CS64

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains A
GAL · beta-D-galactopyranose · sugar · 6 copies · chains A

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

Pockets

3 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	955	0.81	0.82	66	empty
2	273	0.61	0.80	28	empty
3	53	0.49	0.86	16	empty

Compared structures

4TQM · Structural basis of specific recognition of non-reducing terminal N-acetylglucosamine by… · 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 H6CS64
Elsewhere: RCSB PDB 4TQM · PDBe 4TQM · UniProt H6CS64

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