Structure of PDB 4efc Chain B Binding Site BS02

Receptor Information
>4efc Chain B (length=450) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VDYSVDNPLFALSPLDGRYKRQTKALRAFFSEYGFFRYRVLVEVEYFTAL
CKDVPTIVPLRSVTDEQLQKLRKITLDCFSVSSAEEIKRLERVTNHDIKA
VEYFIKERMDTCGLSHVTEFVHFGLTSQDINNTAIPMMIRDAIVTLYLPA
LDGIIGSLTSKLVDWDVPMLARTHGQPASPTNLAKEFVVWIERLREQRRQ
LCEVPTTGKFGGATGNFNAHLVAYPSVNWRAFADMFLAKYLGLKRQQATT
QIENYDHLAALCDACARLHVILIDMCRDVWQYISMGFFKQKVKEGEVGSS
TMPHKVNPIDFENAEGNLALSNALLNFFASKLPISRLQRDLTDSTVLRNL
GVPIGHACVAFASISQGLEKLMISRETISRELSSNWAVVAEGIQTVLRRE
CYPKPYETLKKVTEEQVRNFINGLTDISDDVRAELLAITPFTYVGYVPRF
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 chain4efc Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4efc Crystal Structure of Adenylosuccinate Lyase from Trypanosoma Brucei, Tb427tmp.160.5560
Resolution2.0 Å
Binding residue
(original residue number in PDB)		N106 H107 D108 S138 Q139 R350 L352 S355 T356 R359
Binding residue
(residue number reindexed from 1)		N95 H96 D97 S127 Q128 R339 L341 S344 T345 R348
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H107 T184 H185 S311 K316 E323
Catalytic site (residue number reindexed from 1) H96 T173 H174 S300 K305 E312
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:0046872 metal ion binding
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:0006188 IMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009152 purine ribonucleotide biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0020015 glycosome

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Cellular Component
External links
PDB RCSB:4efc, PDBe:4efc, PDBj:4efc
PDBsum4efc
PubMed
UniProtQ38EJ2

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