Structure of PDB 3lrm Chain C

Receptor sequence
>3lrmC (length=452) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
VSPSYNGLGLTPQMGWDNWNTFACDVSEQLLLDTADRISDLGLKDMGYKY
IILDDCWSSGRDSDGFLVADEQKFPNGMGHVADHLHNNSFLFGMYSSAGE
YTCAGYPGSLGREEEDAQFFANNRVDYLKYANCYNKGQFGTPEISYHRYK
AMSDALNKTGRPVFYSLCNWGQDLTFYWGSGIANSWRMSGDVTAEFTRPD
SRCPCDGDEYDCKYAGFHCSIMNILNKAAPMGQNAGVGGWNDLDNLEVGV
GNLTDDEEKAHFSMWAMVKSPLIIGANVNNLKASSYSIYSQASVIAINQD
SNGIPATRVWRYYVSDTDEYGQGEIQMWSGPLDNGDQVVALLNGGSVSRP
MNTTLEEIFFDSNLGSKKLTSTWDIYDLWANRVDNSTASAILGRNKTATG
ILYNATEQSYKDGLSKNDTRLFGQKIGSLSPNAILNTTVPAHGIAFYRLR
PS
3D structure
PDB3lrm Structural analysis of Saccharomyces cerevisiae alpha-galactosidase and its complexes with natural substrates reveals new insights into substrate specificity of GH27 glycosidases.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A149 D209
Catalytic site (residue number reindexed from 1) A131 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 C C121 W188 C103 W170
BS02 FRU C W37 C121 W19 C103
BS03 GLA C W37 D72 D73 Y113 C121 K147 C186 D209 W19 D54 D55 Y95 C103 K129 C168 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
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Biological Process
External links
PDB RCSB:3lrm, PDBe:3lrm, PDBj:3lrm
PDBsum3lrm
PubMed20592022
UniProtP04824|MEL1_YEASX Alpha-galactosidase 1 (Gene Name=MEL1)

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