Structure of PDB 1eyz Chain B Binding Site BS01

Receptor Information
>1eyz Chain B (length=389) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMH
VAHRSHVINMLDGDALRRVVELEKPHYIVPEIEAIATDMLIQLEEEGLNV
VPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVADIGYP
CIVKPVMSSSGKGQTFIRSAEQLAQAWKYAQQGGRAGRVIVEGVVKFDFE
ITLLTVSAVDGVHFCAPVGHRQEDGDYRESWQPQQMSPLALERAQEIARK
VVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALH
VRAFLGLPVGGIRQYGPAASAVILPQLTSQNVTFDNVQNAVGADLQIRLF
GKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQG
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 chain1eyz Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1eyz Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase.
Resolution1.75 Å
Binding residue
(original residue number in PDB)
E267 E279
Binding residue
(residue number reindexed from 1)
E264 E276
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E115 K155 S160 G162 E267 E279 D286 T287 R363
Catalytic site (residue number reindexed from 1) E114 K154 S159 G161 E264 E276 D283 T284 R360
Enzyme Commision number 6.3.1.21: phosphoribosylglycinamide formyltransferase 2.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004644 phosphoribosylglycinamide formyltransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008776 acetate kinase activity
GO:0016742 hydroxymethyl-, formyl- and related transferase activity
GO:0016874 ligase activity
GO:0043815 phosphoribosylglycinamide formyltransferase 2 activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009152 purine ribonucleotide biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Cellular Component
External links
PDB RCSB:1eyz, PDBe:1eyz, PDBj:1eyz
PDBsum1eyz
PubMed10913290
UniProtP33221|PURT_ECOLI Formate-dependent phosphoribosylglycinamide formyltransferase (Gene Name=purT)

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