Structure of PDB 3lrl Chain A

Receptor sequence
>3lrlA (length=452) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
VSPSYNGLGLTPQMGWDNWNTFACDVSEQLLLDTADRISDLGLKDMGYKY
IILDDCWSSGRDSDGFLVADEQKFPNGMGHVADHLHNNSFLFGMYSSAGE
YTCAGYPGSLGREEEDAQFFANNRVDYLKYDNCYNKGQFGTPEISYHRYK
AMSDALNKTGRPVFYSLCNWGQDLTFYWGSGIANSWRMSGDVTAEFTRPD
SRCPCDGDEYDCKYAGFHCSIMNILNKAAPMGQNAGVGGWNDLDNLEVGV
GNLTDDEEKAHFSMWAMVKSPLIIGANVNNLKASSYSIYSQASVIAINQD
SNGIPATRVWRYYVSDTDEYGQGEIQMWSGPLDNGDQVVALLNGGSVSRP
MNTTLEEIFFDSNLGSKKLTSTWDIYDLWANRVDNSTASAILGRNKTATG
ILYNATEQSYKDGLSKNDTRLFGQKIGSLSPNAILNTTVPAHGIAFYRLR
PS
3D structure
PDB3lrl Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH27 glycosidases.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D149 D209
Catalytic site (residue number reindexed from 1) D131 D191
Enzyme Commision number 3.2.1.22: alpha-galactosidase.
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 C121 D209 C103 D191
BS02 GLA A D73 Y113 C121 K147 D149 C186 R205 D209 D55 Y95 C103 K129 D131 C168 R187 D191
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004557 alpha-galactosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3lrl, PDBe:3lrl, PDBj:3lrl
PDBsum3lrl
PubMed20592022
UniProtP04824|MEL1_YEASX Alpha-galactosidase 1 (Gene Name=MEL1)

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