Structure of PDB 5ixe Chain A

Receptor sequence
>5ixeA (length=485) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence]
MYSFPNSFRFGWSQAGFQSEMGTPGSEDPNTDGYKWVHDPENMAAGLVSG
DLPENGPGYWGNYKTFHDNAQKMGLKIARLNVEWSRIFPNPLPRPQNFDE
SKQDVTEVEINENELKRLDEYANKDALNHYREIFKDLKSRGLYFILNMYH
WPLPLWLHDPIRVRRGDFTGPSGWLSTRTVYEFARFSAYIAWKFDDLVDE
YSTMNEPNVVGGLGYVGVKSGFPPGYLSFELSRRAMYNIIQAHARAYDGI
KSVSKKPVGIIYANSSFQPLTDKDMEAVEMAENDNRWWFFDAIIRGEITK
IVRDDLKGRLDWIGVNYYTRTVVKRTEKGYVSLGGYGHGCERNSVSLAGL
PTSDFGWEFFPEGLYDVLTKYWNRYHLYMYVTENGIADDADYQRPYYLVS
HVYQVHRAINSGADVRGYLHWSLADNYEWASGFSMRFGLLKVDYNTKRLY
WRPSALVYREIATNGAITDEIEHLNSVPPVKPLRH
3D structure
PDB5ixe Full and Partial Agonism of a Designed Enzyme Switch.
ChainA
Resolution1.75 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 H150 E206 V209 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 14O A V37 W151 F222 P223 W433 V37 W151 F222 P223 W429 MOAD: Kd=2.3mM
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:5ixe, PDBe:5ixe, PDBj:5ixe
PDBsum5ixe
PubMed27389009
UniProtP22498|BGAL_SACS2 Beta-galactosidase (Gene Name=lacS)

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