Structure of PDB 2ptr Chain A Binding Site BS02

Receptor Information
>2ptr Chain A (length=454) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MELSSLTAVSPVDGRYGDKVSALRGIFSEYGLLKFRVQVEVRWLQKLAAH
AAIKEVPAFAADAIGYLDAIVASFSEEDAARIKTIERTTNHDVKAVEYFL
KEKVAEIPELHAVSEFIHFACTSEDINNLSHALMLKTARDEVILPYWRQL
IDGLKDLAVQYRDIPLLSRTAGQPATPSTIGKEMANVAYRMERQYRQLNQ
VEILGKINGAVGNYNAHIAAYPEVDWHQFSEEFVTSLGIQWNPYTTQIEP
HDYIAELFDCVARFNTILIDFDRDVWGYIALNHFKQKTIAGEIGSSTMPH
KVNPIDFENSEGNLGLSNAVLQHLASKLPVSRWQRDLTDSTVLRNLGVGI
GYALIAYQSTLKGVSKLEVNRDHLLDELDHNWEVLAEPIQTVMRRYGIEK
PYEKLKELVDAEGMKQFIDGLALPEEEKARLKAMTPANYIGRAITMVDEL
KHHH
Ligand information
Ligand ID2SA
InChIInChI=1S/C14H18N5O11P/c20-7(21)1-5(14(24)25)18-11-8-12(16-3-15-11)19(4-17-8)13-10(23)9(22)6(30-13)2-29-31(26,27)28/h3-6,9-10,13,22-23H,1-2H2,(H,20,21)(H,24,25)(H,15,16,18)(H2,26,27,28)/t5-,6+,9+,10+,13+/m0/s1
InChIKeyOFBHPPMPBOJXRT-VWJPMABRSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)NC(CC(=O)O)C(=O)O
CACTVS 3.341O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(O)=O)n2cnc3c(N[C@@H](CC(O)=O)C(O)=O)ncnc23
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N[C@@H](CC(=O)O)C(=O)O
CACTVS 3.341O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(O)=O)n2cnc3c(N[CH](CC(O)=O)C(O)=O)ncnc23
ACDLabs 10.04O=C(O)CC(C(=O)O)Nc3ncnc1c3ncn1C2OC(C(O)C2O)COP(=O)(O)O
FormulaC14 H18 N5 O11 P
Name2-[9-(3,4-DIHYDROXY-5-PHOSPHONOOXYMETHYL-TETRAHYDRO-FURAN-2-YL)-9H-PURIN-6-YLAMINO]-SUCCINIC ACID;
ADENYLOSUCCINIC ACID
ChEMBL
DrugBankDB04418
ZINCZINC000004096207
PDB chain2ptr Chain B Residue 1200 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2ptr Substrate and Product Complexes of Escherichia coli Adenylosuccinate Lyase Provide New Insights into the Enzymatic Mechanism.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		H91 D92 T122 S123 Q247 R335 L337 S340 T341 R344
Binding residue
(residue number reindexed from 1)		H91 D92 T122 S123 Q247 R335 L337 S340 T341 R344
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H91 T170 A171 K301 E308
Catalytic site (residue number reindexed from 1) H91 T170 A171 K301 E308
Enzyme Commision number 4.3.2.2: adenylosuccinate lyase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004018 N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006188 IMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0006974 DNA damage response
GO:0009152 purine ribonucleotide biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
Cellular Component
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:2ptr, PDBe:2ptr, PDBj:2ptr
PDBsum2ptr
PubMed17531264
UniProtP0AB89|PUR8_ECOLI Adenylosuccinate lyase (Gene Name=purB)

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