Structure of PDB 4eei Chain B Binding Site BS01

Receptor Information
>4eei Chain B (length=423) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIKRYDVAEISKIWADENKYAKMLEVELAILEALEDRMVPKGTAAEIRAR
AQIRPERVDEIEKVTKHDIIAFCTSIAEQFTAETGKFFHFGVTSSDIIDS
ALSLQIRDSMSYVIKDLEALCDSLLTKAEETKEIITMGRSHGMFAEPMSF
GQKFLGAYVEFKRRLKDLKDFQKDGLTVQFSGAVGNYCILTTEDEKKAAD
ILGLPVEEVSTQVIPRDRIAKLISIHGLIASAIERLAVEIRHLHRSDVFE
VYEGFKKNPISTENLTGMARMLRSHVSIALENCVLWHERDISHSSAERFY
LPDNFGIMVYALRRMKNTIDNLVVQRDIIEDRVRSTSAYLSSFYLHFLVA
NTPFMREDCYKIVQQVAFDLESFSKKLQKVMHDEHNIILDIPEMDFEGIK
KTYLKEIDHVFDRSVKARGENLY
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 chain4eei Chain B Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4eei Crystal Structure of Adenylosuccinate Lyase from Francisella tularensis Complexed with AMP and Succinate
Resolution1.921 Å
Binding residue
(original residue number in PDB)		K66 H67 D68 Q212 R301 I303 S306 R310
Binding residue
(residue number reindexed from 1)		K66 H67 D68 Q212 R289 I291 S294 R298
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H67 S140 H141 K268 E275
Catalytic site (residue number reindexed from 1) H67 S140 H141 K256 E263
Enzyme Commision number 4.3.2.2: adenylosuccinate lyase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004018 N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
GO:0016829 lyase activity
GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009152 purine ribonucleotide biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
GO:0044281 small molecule metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4eei, PDBe:4eei, PDBj:4eei
PDBsum4eei
PubMed
UniProtQ5NIQ1

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