Structure of PDB 7brs Chain A

Receptor sequence
>7brsA (length=1021) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
ITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLR
SLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTN
VTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHL
WCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDM
WRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRD
YLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWS
AEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIR
GVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLC
DRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPS
VIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPM
YARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCQYAHAMGNSLGGFAKY
WQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFC
MNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELL
HWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQ
PNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELG
NKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRID
PNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFIS
RKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGP
QENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWR
GDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPS
VSAEFQLSAGRYHYQLVWCQK
3D structure
PDB7brs Two-Dimensional Design Strategy to Construct Smart Fluorescent Probes for the Precise Tracking of Senescence.
ChainA
Resolution2.67 Å
3D
structure
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Enzymatic activity
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 F4X A N102 D201 E461 Y503 Q537 H540 N604 W999 N100 D199 E459 Y501 Q535 H538 N602 W997
BS02 MG A E416 H418 E461 E414 H416 E459
BS03 MG A D15 N18 V21 Q163 D193 D13 N16 V19 Q161 D191
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:7brs, PDBe:7brs, PDBj:7brs
PDBsum7brs
PubMed33624914
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

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