MolNFT v1 · #83553 · protein

Crystal structure analysis of plant exohydrolase

3WLR · Beta-D-glucan exohydrolase isoenzyme exoi: “Crystal structure analysis of plant exohydrolase”. X-ray diffraction, 1 ligand (NAG), 2 pockets (best druggability 0.74). MolNFT v1 #83553 on GenesisL1: 3D structure, binding sites and…

PDB: 3WLR
Type: protein
Length: 607 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-D-glucan exohydrolase isoenzyme exoi
EC: 3.2.1.-
UniProt: Q9XEI3
Ligands: NAG
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-D-glucan exohydrolase isoenzyme exoi (EC 3.2.1.-)	protein	607	38% helix, 13% strand	Q9XEI3

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
GOL · Glycerol · additive · 8 copies · chains A

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

Pockets

2 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	231	0.74	0.88	51	GOL
2	68	0.33	0.76	17	empty

Modifications

Observed in the structure: 3 glycan, 2 disulfide (N-glycosylation, disulfide).

Compared structures

3WLR · Crystal Structure Analysis of Plant Exohydrolase · 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 Q9XEI3
Elsewhere: RCSB PDB 3WLR · PDBe 3WLR · UniProt Q9XEI3

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