Structure of PDB 1uwr Chain B

Receptor sequence
>1uwrB (length=484) Species: 2287 (Saccharolobus solfataricus) [Search protein sequence]
MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDWYKWVHDPENMAAGLVSG
DLPENGPGYWGNYKTFHDNAQKMGLKIARLNVEWSRIFPNPLPRPFDESK
QDVTEVEINENELKRLDEYANKDALNHYREIFKDLKSRGLYFILNMYHWP
LPLWLHDPIRVRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDEYS
TMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQAHARAYDGIKS
VSKKPVGIIYANSSFQPLTDKDMEAVEMAENDNRWWFFDAIIRGEITEKI
VRDDLKGRLDWIGVNYYTRTVVKRTEKGYVSLGGYGHGCERNSVSLAGLP
TSDFGWEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVSH
VYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLKVDYNTKRLYW
RPSALVYREIATNGAITDEIEHLNSVPPVKPLRH
3D structure
PDB1uwr Structural Studies of the Beta-Glycosidase from Sulfolobus Solfataricus in Complex with Covalently and Noncovalently Bound Inhibitors.
ChainB
Resolution2.14 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 N315 Y317 E382
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 GAF B Q18 H150 E206 Y322 E387 W425 E432 W433 F441 Q18 H148 E204 Y317 E382 W420 E427 W428 F436
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
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Biological Process
External links
PDB RCSB:1uwr, PDBe:1uwr, PDBj:1uwr
PDBsum1uwr
PubMed15147194
UniProtP22498|BGAL_SACS2 Beta-galactosidase (Gene Name=lacS)

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