Structure of PDB 3j7h Chain D

Receptor sequence
>3j7hD (length=1022) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQL
RSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYT
NVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFH
LWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQD
MWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELR
DYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLW
SAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLI
RGVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTL
CDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHP
SVIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICP
MYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAK
YWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQF
CMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNEL
LHWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVV
QPNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIEL
GNKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRI
DPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFI
SRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLG
PQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQW
RGDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSP
SVSAEFQLSAGRYHYQLVWCQK
3D structure
PDB3j7h Structure of beta-galactosidase at 3.2- angstrom resolution obtained by cryo-electron microscopy.
ChainD
Resolution3.2 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) D200 H356 H390 E415 H417 E460 Y502 E536 N596 F600 N603
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 D E416 H418 E461 E415 H417 E460
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:3j7h, PDBe:3j7h, PDBj:3j7h
PDBsum3j7h
PubMed25071206
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

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