Structure of PDB 1ao0 Chain C Binding Site BS05
Receptor Information
>1ao0 Chain C (length=455) Species:
1423
(Bacillus subtilis) [
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CGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLI
TEVFQNGELSKVKGKGAIGHVRYATGYENVQPLLFRSQNNGSLALAHNGN
LVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNSLSML
KGAYAFLIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDVVGAT
YLREVEPGEMLIINDEGMKSERFSMNINRSICSMEYIYFSRPDSNIDGIN
VHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYELGLI
KNRYVGRTFIQPSQALREQGVRMKLSAVRGVVEGKRVVMVDDSIVRGTTS
RRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHSVEEI
RQEIGADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIYQDTV
LPHVK
Ligand information
Ligand ID
ADP
InChI
InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey
XTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341
Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04
O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341
Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
Formula
C10 H15 N5 O10 P2
Name
ADENOSINE-5'-DIPHOSPHATE
ChEMBL
CHEMBL14830
DrugBank
DB16833
ZINC
ZINC000012360703
PDB chain
1ao0 Chain D Residue 468 [
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Receptor-Ligand Complex Structure
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PDB
1ao0
Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
I304 R307
Binding residue
(residue number reindexed from 1)
I300 R303
Annotation score
2
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
PDBsum
1ao0
PubMed
9271502
UniProt
P00497
|PUR1_BACSU Amidophosphoribosyltransferase (Gene Name=purF)
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