Structure of PDB 6lgf Chain A

Receptor sequence

>6lgfA (length=565) Species: 7091 (Bombyx mori)

VIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAGVDAIW
MSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLKVLLDF
VPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPSNWVSQ
FGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFWLDKGA
DGFRLNALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPLYTKDL
IELYDVVYEWREFLDEYNKNHGGDTRVVFSEGYANVSMTMLYYGNEDGAI
GAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFGNHDNN
RMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDTVDIEA
CNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDYQEINL
AKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVRSLPTH
DTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEITSSQL
SLEAGEALVLKAQPI

3D structure

• PDB: 6lgf Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
• Chain: A
• Resolution: 1.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D140 N247 E322 H388 D389
• Catalytic site (residue number reindexed from 1): D99 N206 E281 H347 D348
• Enzyme Commision number: 3.2.1.20: alpha-glucosidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	GLC	A	D102 Y105 H145 F211 N247 E322 H388 D389 R455	D61 Y64 H104 F170 N206 E281 H347 D348 R414
BS02	FRU	A	F211 E322 Y324 D389 E440	F170 E281 Y283 D348 E399
BS03	MG	A	D63 D65 D67 I69 D71	D22 D24 D26 I28 D30
BS04	CA	A	N144 D217 Y251 L252 E254	N103 D176 Y210 L211 E213

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:6lgf, PDBe:6lgf, PDBj:6lgf
• PDBsum: 6lgf
• PubMed: 32381508
• UniProt: A0A077JI83