Structure of PDB 6lgb Chain A

Receptor sequence
>6lgbA (length=565) Species: 7091 (Bombyx mori) [Search protein sequence]
VIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAGVDAIW
MSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLKVLLDF
VPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPSNWVSQ
FGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFWLDKGA
DGFRLDALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPLYTKDL
IELYDVVYEWREFLDEYNKNHGGDTRVVFSEGYANVSMTMLYYGNEDGAI
GAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFGNHDNN
RMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDTVDIEA
CNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDYQEINL
AKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVRSLPTH
DTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEITSSQL
SLEAGEALVLKAQPI
3D structure
PDB6lgb Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D140 D247 E322 H388 D389
Catalytic site (residue number reindexed from 1) D99 D206 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 MG A D63 D65 D67 I69 D71 D22 D24 D26 I28 D30
BS02 CA A N144 D217 Y251 L252 E254 N103 D176 Y210 L211 E213
BS03 GLC A D102 Y105 H145 F211 E322 H388 D389 R455 D61 Y64 H104 F170 E281 H347 D348 R414
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6lgb, PDBe:6lgb, PDBj:6lgb
PDBsum6lgb
PubMed32381508
UniProtA0A077JI83

[Back to BioLiP]