Structure of PDB 1jz4 Chain D

Receptor sequence

>1jz4D (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: 1jz4 A Structural View of the Action of Escherichia Coli (Lacz) Beta-Galactosidase
• Chain: D
• Resolution: 2.1 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	2DG	D	D201 H391 E461 M502 Y503 E537 H540 W568	D189 H379 E449 M490 Y491 E525 H528 W556
BS02	MG	D	E416 H418 E461	E404 H406 E449
BS03	MG	D	D15 N18 V21 Q163 D193	D3 N6 V9 Q151 D181
BS04	NA	D	D201 F601 N604	D189 F589 N592
BS05	NA	D	F556 Y559 P560 L562	F544 Y547 P548 L550
BS06	NA	D	F931 P932 L967 M968 T970	F919 P920 L955 M956 T958

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:1jz4, PDBe:1jz4, PDBj:1jz4
• PDBsum: 1jz4
• PubMed: 11732897
• UniProt: P00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)