Structure of PDB 3t0b Chain A Binding Site BS02

Receptor Information
>3t0b Chain A (length=1014) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR
FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITV
NPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWV
GYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIF
RDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVS
LWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLY
RAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH
HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYV
VDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLG
NESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDED
QPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQY
PRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFA
DRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD
GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWS
EAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFN
RQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVTEATRIDPNAWVER
WKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRID
GSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDR
LTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI
SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQL
SAGRYHYQLVWCQK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3t0b Chain A Residue 3002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3t0b er-796 of Beta-Galactosidase (E. coli) Plays a Key Role in Maintaining an Optimum Balance between the Opened and Closed Conformations of the Catalytically Important Active Site Loop
Resolution2.4 Å
Binding residue
(original residue number in PDB)		D15 N18 V21 Q163 D193
Binding residue
(residue number reindexed from 1)		D6 N9 V12 Q154 D184
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D201 H357 H391 E416 H418 E461 Y503 E537 N597 F601 N604
Catalytic site (residue number reindexed from 1) D192 H348 H382 E407 H409 E452 Y494 E528 N588 F592 N595
Enzyme Commision number 3.2.1.23: beta-galactosidase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
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:0031420 alkali metal ion binding
GO:0042802 identical protein 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
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Biological Process
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Cellular Component
External links
PDB RCSB:3t0b, PDBe:3t0b, PDBj:3t0b
PDBsum3t0b
PubMed22155115
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

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