Structure of PDB 1jyx Chain B

Receptor sequence

>1jyxB (length=1011) Species: 562 (Escherichia coli)

RRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAW
FPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPP
FVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYG
QDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDV
SLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQ
GETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAV
VELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHPL
HGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDE
ANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNES
GHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDEDQPF
PAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPRL
QGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFADRT
PHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALDGKP
LASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAG
HISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQS
GFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKA
AGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRIDGSG
QMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDRLTA
ACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISRY
SQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAG
RYHYQLVWCQK

3D structure

• PDB: 1jyx A Structural View of the Action of Escherichia Coli (Lacz) Beta-Galactosidase
• Chain: B
• Resolution: 1.75 Å

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): D189 H345 H379 E404 H406 E449 Y491 E525 N585 F589 N592
• 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	B	E416 H418 E461	E404 H406 E449
BS02	MG	B	D15 N18 V21 Q163 D193	D3 N6 V9 Q151 D181
BS03	NA	B	D201 F601 N604	D189 F589 N592
BS04	NA	B	F556 Y559 P560 L562 Q563	F544 Y547 P548 L550 Q551
BS05	NA	B	F931 P932 L967 M968 T970	F919 P920 L955 M956 T958
BS06	NA	B	S647 D648 N649 E650 L670	S635 D636 N637 E638 L658
BS07	IPT	B	N102 D201 E461 E537 H540 W999	N90 D189 E449 E525 H528 W987	BindingDB: Ki=7.6e+4nM

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

External links

• PDB: RCSB:1jyx, PDBe:1jyx, PDBj:1jyx
• PDBsum: 1jyx
• PubMed: 11732897
• UniProt: P00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)