Structure of PDB 1jz4 Chain C

Receptor sequence

>1jz4C (length=1011) Species: 562 (Escherichia coli) [Search protein sequence]

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

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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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	C	D201 H391 E461 Y503 E537 H540 W568	D189 H379 E449 Y491 E525 H528 W556
BS02	MG	C	E416 H418 E461	E404 H406 E449
BS03	MG	C	D15 N18 V21 Q163 D193	D3 N6 V9 Q151 D181
BS04	NA	C	D201 F601 N604	D189 F589 N592
BS05	NA	C	F556 Y559 P560 L562	F544 Y547 P548 L550
BS06	NA	C	F931 P932 L967 M968 T970	F919 P920 L955 M956 T958
BS07	NA	C	S647 D648 E650 L670	S635 D636 E638 L658

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

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