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Streptomyces lividans endoglucanase (ec: 3.2.1.4) complex with modified glucose trimer

Analyse Streptomyces lividans endoglucanase (ec: 3.2.1.4) complex with modified glucose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NLR
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (endoglucanase (E.C.3.2.1.4))
EC: 3.2.1.4
Ligands: SHG, BGC
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (endoglucanase (E.C.3.2.1.4)) (EC 3.2.1.4)	protein	222	6% helix, 50% strand	—

Ligands and binding sites

SHG · 2-deoxy-2-fluoro-beta-D-glucopyranose · ligand · chains A
BGC · beta-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	193	0.58	0.80	31	SHG, BGC

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2NLR · Streptomyces lividans endoglucanase (ec: 3.2.1.4) complex with modified glucose trimer · 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
Elsewhere: RCSB PDB 2NLR · PDBe 2NLR

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