MolNFT v1 · #15996 · protein

Endo-1,4-beta-glucanase CELB2, cellulase, native structure

1NLR: “Endo-1,4-beta-glucanase CELB2, cellulase, native structure”. X-ray diffraction, 1 pocket (best druggability 0.48). MolNFT v1 #15996 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1NLR
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-glucanase
EC: 3.2.1.4
UniProt: Q54331
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-glucanase (EC 3.2.1.4)	protein	222	5% helix, 50% strand	Q54331

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	165	0.48	0.77	27	empty

Modifications

Observed in the structure: 2 disulfide, 1 modified (disulfide, oxidation).

Compared structures

1NLR · Endo-1,4-beta-glucanase CELB2, cellulase, native structure · 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 Q54331
Elsewhere: RCSB PDB 1NLR · PDBe 1NLR · UniProt Q54331

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