Structure of PDB 1gph Chain 3 Binding Site BS02

Receptor Information
>1gph Chain 3 (length=465) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLI
TEVFQNGELSKVKGKGAIGHVRYATAGGGGYENVQPLLFRSQNNGSLALA
HNGNLVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNS
LSMLKGAYAFLIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDV
VGATYLREVEPGEMLIINDEGMKSERFSMNINRSICSMEYIYFSRPDSNI
DGINVHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYE
LGLIKNRYVGRTFIQPSQALREQGVRMKLSAVRGVVEGKRVVMVDDSIVR
GTTSRRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHS
VDEIRQEIGADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIY
QDTVLPHVKEAVLTK
Ligand information
Ligand IDAMP
InChIInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyUDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
FormulaC10 H14 N5 O7 P
NameADENOSINE MONOPHOSPHATE
ChEMBLCHEMBL752
DrugBankDB00131
ZINCZINC000003860156
PDB chain1gph Chain 3 Residue 467 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1gph Structure of the allosteric regulatory enzyme of purine biosynthesis.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		M238 Y242 S283 D345 D346 S347 V349 R350 G351 T352 T353
Binding residue
(residue number reindexed from 1)		M238 Y242 S283 D345 D346 S347 V349 R350 G351 T352 T353
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) E300 K305 Q315 K423
Catalytic site (residue number reindexed from 1) E300 K305 Q315 K423
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:1gph, PDBe:1gph, PDBj:1gph
PDBsum1gph
PubMed8197456
UniProtP00497|PUR1_BACSU Amidophosphoribosyltransferase (Gene Name=purF)

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