Structure of PDB 1uws Chain B

Receptor sequence
>1uwsB (length=485) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDPENMAAGLVSG
DLPENGPGYWGNYKTFHDNAQKMGLKIARLNVEWSRIFPNPLPRPFDESK
QDVTEVEINENELKRLDEYANKDALNHYREIFKDLKSRGLYFILNMYHWP
LPLWLHDPIRVRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDEYS
TMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQAHARAYDGIKS
VSKKPVGIIYANSSFQPLTDKDMEAVEMAENDNRWWFFDAIIRGEITREK
IVRDDLKGRLDWIGVNYYTRTVVKRTEKGYVSLGGYGHGCERNSVSLAGL
PTSDFGWEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVS
HVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLKVDYNTKRLY
WRPSALVYREIATNGAITDEIEHLNSVPPVKPLRH
3D structure
PDB1uws Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R79 H150 E206 V209 N320 Y322 E387
Catalytic site (residue number reindexed from 1) R79 H148 E204 V207 N316 Y318 E383
Enzyme Commision number 3.2.1.23: beta-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 G2F B Q18 H150 N205 E206 Y322 E387 W425 E432 F441 Q18 H148 N203 E204 Y318 E383 W421 E428 F437
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1uws, PDBe:1uws, PDBj:1uws
PDBsum1uws
PubMed15147194
UniProtP22498|BGAL_SACS2 Beta-galactosidase (Gene Name=lacS)

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