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Crystal structure of glucoamylase from saccharomycopsis fibuligera at 1.7 ångströms

Analyse Crystal structure of glucoamylase from saccharomycopsis fibuligera at 1.7… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AYX
Type: protein
Length: 492 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucoamylase
EC: 3.2.1.3
UniProt: P08017
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucoamylase (EC 3.2.1.3)	protein	492	51% helix, 7% strand	P08017

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	159	0.66	0.87	34	empty
2	126	0.56	0.83	25	TRS
3	87	0.45	0.80	18	empty

Compared structures

1AYX · Crystal structure of glucoamylase from saccharomycopsis fibuligera at 1.7 ångströms · the same entry in another collection · chain A against A, TM-score 1.00
P08017 · AlphaFold monomer V2.0 prediction for glucoamylase GLU1 (P08017) · a predicted model of the same protein · 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 P08017
Elsewhere: RCSB PDB 1AYX · PDBe 1AYX · UniProt P08017

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