Structure of PDB 6lgi Chain A

Receptor sequence

>6lgiA (length=570) Species: 7091 (Bombyx mori)

PPPTEVIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAG
VDAIWMSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLK
VLLDFVPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPS
NWVSQFGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFW
LDKGADGFRLDALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPL
YTKDLIELYDVVYEWREFLDEYNKNHGGDTRVVFSQGYANVSMTMLYYGN
EDGAIGAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFG
NHDNNRMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDT
VDIEACNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDY
QEINLAKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVR
SLPTHDTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEI
TSSQLSLEAGEALVLKAQPI

3D structure

• PDB: 6lgi Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
• Chain: A
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D140 D247 Q322 H388 D389
• Catalytic site (residue number reindexed from 1): D104 D211 Q286 H352 D353
• 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	MG	A	D63 D65 D67 I69 D71	D27 D29 D31 I33 D35
BS02	CA	A	N144 D217 Y251 L252 E254	N108 D181 Y215 L216 E218
BS03	BGC	A	D102 Y105 H145 F211 R245 D247 H388 D389 R455	D66 Y69 H109 F175 R209 D211 H352 D353 R419
BS04	FRU	A	Q322 Y324 D389 E440	Q286 Y288 D353 E404
BS05	BDF	A	F220 R221 K226 I253 D296 E300	F184 R185 K190 I217 D260 E264

Gene Ontology

Molecular Function

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

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

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