Structure of PDB 4duv Chain C

Receptor sequence
>4duvC (length=1018) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
IDPVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLN
GEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTY
PITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCN
GRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRM
SGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLR
VTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEI
PNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVN
RHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRY
GLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVII
WSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYAR
VDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQA
FRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNG
LVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWM
VALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNA
TAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKR
WQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIAVSEATRIDPNA
WVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKT
YRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQEN
YPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDF
QFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSA
EFQLSAGRYHYQLVWCQK
3D structure
PDB4duv The Glucose Acceptor site of lacZ beta-galactosidase for the synthesis of allolactose - the natural inducer of the lac operon
ChainC
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) D196 H352 H386 E411 H413 E456 Y498 E532 N592 F596 N599
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 2DG C D201 H391 E461 Y503 E537 H540 W568 F601 D196 H386 E456 Y498 E532 H535 W563 F596
BS02 MG C E416 H418 E461 E411 H413 E456
BS03 MG C D15 N18 V21 Q163 D193 D10 N13 V16 Q158 D188
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4duv, PDBe:4duv, PDBj:4duv
PDBsum4duv
PubMed
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

[Back to BioLiP]