Structure of PDB 2j91 Chain B Binding Site BS01

Receptor Information
>2j91 Chain B (length=463) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLG
LPITDEQIREMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCAAGII
HLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLG
FTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQA
SFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLA
SLGASVHKICTDIRLLANLKEMEEPFMPYKRNPMRSERCCSLARHLMTLV
MDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVY
PKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVK
QEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEV
YPLLKPYESVKAE
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 chain2j91 Chain B Residue 1000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2j91 Crystal Structure of Human Adenylosuccinate Lyase
Resolution1.8 Å
Binding residue
(original residue number in PDB)		R20 Y21 M299 R303
Binding residue
(residue number reindexed from 1)		R16 Y17 M284 R288
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H86 T158 H159 K295 E302
Catalytic site (residue number reindexed from 1) H82 T152 H153 K280 E287
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:0016829 lyase activity
GO:0042802 identical protein binding
GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Biological Process
GO:0001666 response to hypoxia
GO:0006164 purine nucleotide biosynthetic process
GO:0006167 AMP biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0007584 response to nutrient
GO:0009060 aerobic respiration
GO:0009152 purine ribonucleotide biosynthetic process
GO:0009168 purine ribonucleoside monophosphate biosynthetic process
GO:0014850 response to muscle activity
GO:0042594 response to starvation
GO:0044208 'de novo' AMP biosynthetic process
GO:0044209 AMP salvage
GO:0097294 'de novo' XMP biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2j91, PDBe:2j91, PDBj:2j91
PDBsum2j91
PubMed
UniProtP30566|PUR8_HUMAN Adenylosuccinate lyase (Gene Name=ADSL)

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