Structure of PDB 3vda Chain A

Receptor sequence
>3vdaA (length=1015) Species: 562 (Escherichia coli) [Search protein sequence]
VVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEW
RFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPIT
VNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRW
VGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGI
FRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTV
SLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNL
YRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHE
HHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLY
VVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSL
GTESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDE
DQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQ
YPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVF
ADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVAL
DGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAW
SEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQF
NRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVE
RWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRI
DGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPD
RLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFN
ISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQ
LSAGRYHYQLVWCQK
3D structure
PDB3vda Substitution for Asn460 cripples {beta}-galactosidase (Escherichia coli) by increasing substrate affinity and decreasing transition state stability.
ChainA
Resolution2.5 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) D193 H349 H383 E408 H410 E453 Y495 E529 N589 F593 N596
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 MG A E416 H418 E461 E408 H410 E453
BS02 MG A D15 N18 V21 Q163 D193 D7 N10 V13 Q155 D185
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:3vda, PDBe:3vda, PDBj:3vda
PDBsum3vda
PubMed22446164
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

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