Structure of PDB 6lgg Chain B

Receptor sequence

>6lggB (length=569) Species: 7091 (Bombyx mori)

PPTEVIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAGV
DAIWMSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLKV
LLDFVPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPSN
WVSQFGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFWL
DKGADGFRLDALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPLY
TKDLIELYDVVYEWREFLDEYNKNHGGDTRVVFSQGYANVSMTMLYYGNE
DGAIGAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFGN
HDNNRMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDTV
DIEACNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDYQ
EINLAKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVRS
LPTHDTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEIT
SSQLSLEAGEALVLKAQPI

3D structure

• PDB: 6lgg Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
• Chain: B
• Resolution: 1.84 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D140 D247 Q322 H388 D389
• Catalytic site (residue number reindexed from 1): D103 D210 Q285 H351 D352
• 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	B	D102 Y105 H145 F211 D247 Q322 H388 D389 R455	D65 Y68 H108 F174 D210 Q285 H351 D352 R418
BS02	FRU	B	A248 Q322 Y324 D389 E440	A211 Q285 Y287 D352 E403
BS03	MG	B	D63 D65 D67 I69 D71	D26 D28 D30 I32 D34
BS04	CA	B	N144 D217 Y251 L252 E254	N107 D180 Y214 L215 E217

Gene Ontology

Molecular Function

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

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

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