Structure of PDB 4v41 Chain G

Receptor sequence
>4v41G (length=1021) Species: 511693 (Escherichia coli BL21) [Search protein sequence]
ITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLR
SLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTN
VTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHL
WCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDM
WRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRD
YLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWS
AEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIR
GVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLC
DRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPS
VIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPM
YARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKY
WQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFC
MNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELL
HWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQ
PNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELG
NKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRID
PNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFIS
RKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGP
QENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWR
GDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPS
VSAEFQLSAGRYHYQLVWCQK
3D structure
PDB4v41 High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation.
ChainG
Resolution2.5 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) D199 H355 H389 E414 H416 E459 Y501 E535 N595 F599 N602
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 G E416 H418 E461 E414 H416 E459
BS02 MG G D15 N18 V21 Q163 D193 D13 N16 V19 Q161 D191
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:4v41, PDBe:4v41, PDBj:4v41
PDBsum4v41
PubMed11045615
UniProtP00722|BGAL_ECOLI Beta-galactosidase (Gene Name=lacZ)

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