Structure of PDB 3t2p Chain A

Receptor sequence
>3t2pA (length=1014) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
VLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR
FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITV
NPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWV
GYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIF
RDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVS
LWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLY
RAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH
HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYV
VDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLG
NESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDED
QPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQY
PRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFA
DRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD
GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWS
EAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFN
RQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVDEATRIDPNAWVER
WKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRID
GSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDR
LTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI
SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQL
SAGRYHYQLVWCQK
3D structure
PDB3t2p Ser-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
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 IPT A D201 E461 Y503 E537 H540 N604 W999 D192 E452 Y494 E528 H531 N595 W990 PDBbind-CN: -logKd/Ki=3.60,Ki=0.25mM
BindingDB: Ki=7.6e+4nM
BS02 MG A E416 H418 E461 E407 H409 E452
BS03 MG A D15 N18 V21 Q163 D193 D6 N9 V12 Q154 D184
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:3t2p, PDBe:3t2p, PDBj:3t2p
PDBsum3t2p
PubMed22155115
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

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