Structure of PDB 1f4a Chain D Binding Site BS02

Receptor Information
>1f4a Chain D (length=1021) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLR
SLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTN
VTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHL
WCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDM
WRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRD
YLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWS
AEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIR
GVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLC
DRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPS
VIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPM
YARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKY
WQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFC
MNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELL
HWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQ
PNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELG
NKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRID
PNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFIS
RKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGP
QENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWR
GDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPS
VSAEFQLSAGRYHYQLVWCQK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1f4a Chain D Residue 3002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1f4a High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		D15 N18 V21 Q163 D193
Binding residue
(residue number reindexed from 1)		D13 N16 V19 Q161 D191
Annotation score4
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) D199 H355 H389 E414 H416 E459 Y501 E535 N595 F599 N602
Enzyme Commision number 3.2.1.23: beta-galactosidase.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1f4a, PDBe:1f4a, PDBj:1f4a
PDBsum1f4a
PubMed11045615
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

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