Structure of PDB 6tte Chain D

Receptor sequence
>6tteD (length=1014) Species: 562 (Escherichia coli) [Search protein sequence]
VLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR
FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITV
NPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWV
GYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIF
RDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVS
LWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLY
RAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH
HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYV
VDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLG
NESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDED
QPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQY
PRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFA
DRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD
GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWS
EAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFN
RQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVER
WKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRID
GSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDR
LTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI
SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQL
SAGRYHYQLVWCQK
3D structure
PDB6tte Fragment-based drug discovery using cryo-EM.
ChainD
Resolution2.2 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 MG D E416 H418 E461 E407 H409 E452
BS02 PTQ D N102 D201 E461 E537 H540 D598 F601 N604 W999 N93 D192 E452 E528 H531 D589 F592 N595 W990
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:6tte, PDBe:6tte, PDBj:6tte
PDBsum6tte
PubMed31877353
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

[Back to BioLiP]