Structure of PDB 1ecj Chain C Binding Site BS01

Receptor Information
>1ecj Chain C (length=492) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGL
VSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAH
NGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEAD
NIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDEN
RTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSN
PCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIP
IPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKL
NANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIR
FPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAEN
PDIQQFECSVFNGVYVTKDVDQGYLDFLDTLRNDDAKAVQRQ
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 chain1ecj Chain C Residue 505 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ecj Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		Y74 Y258 D366 D367 S368 V370 R371 G372 T374
Binding residue
(residue number reindexed from 1)		Y74 Y258 D366 D367 S368 V370 R371 G372 T374
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) C1 G27 N101 G102 Y258 R321 K326 M336 D444
Catalytic site (residue number reindexed from 1) C1 G27 N101 G102 Y258 R321 K326 M336 D444
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:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0097216 guanosine tetraphosphate 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
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ecj, PDBe:1ecj, PDBj:1ecj
PDBsum1ecj
PubMed9514258
UniProtP0AG16|PUR1_ECOLI Amidophosphoribosyltransferase (Gene Name=purF)

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