Structure of PDB 5foo Chain B

Receptor sequence
>5fooB (length=463) Species: 160490 (Streptococcus pyogenes M1 GAS) [Search protein sequence]
MLAFPKEFWWGGATSGPQSEGRFAKQHRNLFDYWYEEEPDLFYDYVGPDT
ASDAYHQIESDLTLLASLGHNSYRTSIQWTRLIDDFEQATINPDGLAYYN
RVIDACLANGIRPVINLHHFDLPIALYQAYGGWESKHVVDLFVAFSKVCF
EQFGDRVKDWFVHNEPMVVVEGSYLMQFHYPAIVDGKKAVQVAYNLALAT
AKVIQAYRRGPAELSDGRIGTILNLTPAYPASQSEADMAAAHFAELWNND
LFMEAAVHGKFPEELVAVLKKDGVLWQSTPEELALIAENRVDYLGLNFYH
PKRVKAPDAIPVISPSWSPEWYYDPYLMPGHRMNVDKGWEIYPEAVYDIA
IKMRDHYDNIPWFLSENGVGISGEDRYRDETGQIQDDYRIQFLKEHLTYL
HKGIEAGSNCFGYHVWTPIDGWSWLNAYKNRYGLVENNIHTQVRRPKASA
YWFKKVATHNRLI
3D structure
PDB5foo Chemoenzymatic Synthesis of 6-Phospho-Cyclophellitol as a Novel Probe of 6-Phospho-Beta-Glucosidases.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R74 H119 E165 V168 N297 Y299 E366
Catalytic site (residue number reindexed from 1) R74 H119 E165 V168 N297 Y299 E366
Enzyme Commision number '3.2.1.21
3.2.1.86'
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 JAZ B Q18 H119 Y299 K337 E366 W416 S423 W424 Y432 Q18 H119 Y299 K337 E366 W416 S423 W424 Y432
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0016052 carbohydrate catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5foo, PDBe:5foo, PDBj:5foo
PDBsum5foo
PubMed26790390
UniProtQ99YP9

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