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DEX49A from penicillium minioluteum complex with isomaltose

Analyse DEX49A from penicillium minioluteum complex with isomaltose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OGO
Type: protein
Length: 572 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dextranase
EC: 3.2.1.11
UniProt: P48845
Ligands: BGC, GLC
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Dextranase (EC 3.2.1.11)	protein	572	3% helix, 42% strand	P48845

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · chains X
GLC · alpha-D-glucopyranose · sugar · chains X

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	274	0.55	0.76	26	GLC
2	72	0.53	0.86	16	empty
3	63	0.33	0.76	17	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1OGO · Dex49A from Penicillium minioluteum complex with isomaltose · the same entry in another collection · chain X against X, TM-score 1.00
P48845 · AlphaFold monomer V2.0 prediction for dextranase (P48845) · a predicted model of the same protein · chain X 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 P48845
Elsewhere: RCSB PDB 1OGO · PDBe 1OGO · UniProt P48845

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