Structure of PDB 1ao0 Chain D Binding Site BS02

Receptor Information
>1ao0 Chain D (length=455) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLI
TEVFQNGELSKVKGKGAIGHVRYATGYENVQPLLFRSQNNGSLALAHNGN
LVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNSLSML
KGAYAFLIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDVVGAT
YLREVEPGEMLIINDEGMKSERFSMNINRSICSMEYIYFSRPDSNIDGIN
VHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYELGLI
KNRYVGRTFIQPSQALREQGVRMKLSAVRGVVEGKRVVMVDDSIVRGTTS
RRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHSVEEI
RQEIGADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIYQDTV
LPHVK
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 chain1ao0 Chain D Residue 469 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ao0 Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		S283 D345 D346
Binding residue
(residue number reindexed from 1)		S279 D341 D342
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C1 G27 N102 G103 Y242 E300 K305 Q315 K423
Catalytic site (residue number reindexed from 1) C1 G27 N98 G99 Y238 E296 K301 Q311 K419
Enzyme Commision number 2.4.2.14: amidophosphoribosyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004044 amidophosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0006541 glutamine metabolic process
GO:0009113 purine nucleobase biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ao0, PDBe:1ao0, PDBj:1ao0
PDBsum1ao0
PubMed9271502
UniProtP00497|PUR1_BACSU Amidophosphoribosyltransferase (Gene Name=purF)

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