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Crystal structure of bacterial glucoamylase

Analyse Crystal structure of bacterial glucoamylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LF6
Type: protein
Length: 1,348 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucoamylase
EC: 3.2.1.3
UniProt: O85672
Ligands: SO4
Pockets: 7 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glucoamylase (EC 3.2.1.3)	protein	674	35% helix, 24% strand	O85672

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	617	0.79	0.84	74	SO4
2	209	0.67	0.85	31	empty
3	216	0.66	0.84	36	empty
4	320	0.55	0.75	48	empty
5	279	0.53	0.76	46	empty

Interfaces

1 interface between chains.

A–B · 615 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1LF6 · Crystal structure of bacterial glucoamylase · 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 O85672
Elsewhere: RCSB PDB 1LF6 · PDBe 1LF6 · UniProt O85672

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