Structure of PDB 1jwa Chain B Binding Site BS01

Receptor Information
>1jwa Chain B (length=217) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AELSDQEMLRYNRQIILRGFDFDGQEALKDSRVLIVGLGGLGCAASQYLA
SAGVGNLTLLDFDTVSLSNLQRQTLHSDATVGQPKVESARDALTRINPHI
AITPVNALLDDAELAALIAEHDLVLDCTDNVAVRNQLNAGCFAAKVPLVS
GAAIRMEGQITVFTYEAGVMAPLIGVIGSLQAMEAIKMLAGYGKPASGKI
VMYDAMTCQFREMKLMR
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain1jwa Chain B Residue 250 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1jwa Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		G40 G41 D62 F63 R73 K86 L109 D130 N131 V134
Binding residue
(residue number reindexed from 1)		G39 G40 D61 F62 R72 K85 L108 D129 N130 V133
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R14 D130
Catalytic site (residue number reindexed from 1) R13 D129
Enzyme Commision number 2.7.7.80: molybdopterin-synthase adenylyltransferase.
Gene Ontology
Molecular Function
GO:0004792 thiosulfate sulfurtransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008146 sulfotransferase activity
GO:0008641 ubiquitin-like modifier activating enzyme activity
GO:0016779 nucleotidyltransferase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0061605 molybdopterin-synthase adenylyltransferase activity
Biological Process
GO:0006777 Mo-molybdopterin cofactor biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:1990133 molybdopterin adenylyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jwa, PDBe:1jwa, PDBj:1jwa
PDBsum1jwa
PubMed11713534
UniProtP12282|MOEB_ECOLI Molybdopterin-synthase adenylyltransferase (Gene Name=moeB)

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