Structure of PDB 6tsk Chain B Binding Site BS02

Receptor Information
>6tsk Chain B (length=1015) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEW
RFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPIT
VNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRW
VGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGI
FRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTV
SLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNL
YRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHE
HHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLY
VVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSL
GNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDE
DQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQ
YPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVF
ADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVAL
DGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAW
SEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQF
NRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVE
RWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRI
DGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPD
RLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFN
ISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQ
LSAGRYHYQLVWCQK
Ligand information
Ligand ID0MK
InChIInChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3-,4-,5-/m0/s1
InChIKeySRBFZHDQGSBBOR-FCAWWPLPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C1C(C(C(C(O1)O)O)O)O
OpenEye OEToolkits 1.7.6C1[C@@H]([C@@H]([C@@H]([C@H](O1)O)O)O)O
CACTVS 3.385O[CH]1CO[CH](O)[CH](O)[CH]1O
ACDLabs 12.01C1(O)C(O)C(O)C(CO1)O
CACTVS 3.385O[C@H]1CO[C@H](O)[C@@H](O)[C@H]1O
FormulaC5 H10 O5
Namebeta-L-ribopyranose;
beta-L-ribose;
L-ribose;
ribose;
L-ribopyranose
ChEMBL
DrugBank
ZINCZINC000004521829
PDB chain6tsk Chain B Residue 3002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6tsk Fragment-based drug discovery using cryo-EM.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		D201 E461 Y503 E537 H540 W568 F601
Binding residue
(residue number reindexed from 1)		D193 E453 Y495 E529 H532 W560 F593
Annotation score4
Enzymatic activity
Enzyme Commision number 3.2.1.23: beta-galactosidase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005990 lactose catabolic process
GO:0009056 catabolic process
Cellular Component
GO:0009341 beta-galactosidase complex

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6tsk, PDBe:6tsk, PDBj:6tsk
PDBsum6tsk
PubMed31877353
UniProtL0N6M2

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