Structure of PDB 7btk Chain A

Receptor sequence
>7btkA (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
PDB7btk Two-Dimensional Design Strategy to Construct Smart Fluorescent Probes for the Precise Tracking of Senescence.
ChainA
Resolution2.7 Å
3D
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
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 F6L A N102 D201 H391 N460 E461 Y503 F512 Q537 H540 W568 W999 N100 D199 H389 N458 E459 Y501 F510 Q535 H538 W566 W997
BS02 MG A D201 E416 H418 E461 D199 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:7btk, PDBe:7btk, PDBj:7btk
PDBsum7btk
PubMed33624914
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

[Back to BioLiP]