Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

Structure of PDB 3dl0 Chain B Binding Site BS02

Receptor Information >3dl0 Chain B (length=216) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] MNLVLMGLPGAGKGTQGERIVEKYGIPHISTGDMFRAAMKEETPLGLEAK SYIDKGELVPDEVTIGIVKERLGKDDCERGFLLDGFPRTVAQAEALEEIL EEMGKPIDYVINIQVDKDVLMERLTGRRICSVCGTTYHLVFNPPKTPGIC DKDGGELYQRADDNEETVTKRLEVNMKQTAPLLDFYDEKGYLVNVNGQQD IQDVYADLKVLLGGLK

Ligand information Ligand ID AP5 InChI InChI=1S/C20H29N10O22P5/c21-15-9-17(25-3-23-15)29(5-27-9)19-13(33)11(31)7(47-19)1-45-53(35,36)49-55(39,40)51-57(43,44)52-56(41,42)50-54(37,38)46-2-8-12(32)14(34)20(48-8)30-6-28-10-16(22)24-4-26-18(10)30/h3-8,11-14,19-20,31-34H,1-2H2,(H,35,36)(H,37,38)(H,39,40)(H,41,42)(H,43,44)(H2,21,23,25)(H2,22,24,26)/t7-,8-,11-,12-,13-,14-,19-,20-/m1/s1 InChIKey OIMACDRJUANHTJ-XPWFQUROSA-N SMILES Software SMILES OpenEye OEToolkits 1.5.0 c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)OP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)n5cnc6c5ncnc6N)O)O)O)O)N CACTVS 3.341 Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)O[P@](O)(=O)O[P@](O)(=O)O[P@](O)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)n5cnc6c(N)ncnc56)[C@@H](O)[C@H]3O OpenEye OEToolkits 1.5.0 c1nc(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[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)n5cnc6c5ncnc6N)O)O)O)O)N CACTVS 3.341 Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(=O)O[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH]([CH](O)[CH]4O)n5cnc6c(N)ncnc56)[CH](O)[CH]3O Formula C20 H29 N10 O22 P5 Name BIS(ADENOSINE)-5'-PENTAPHOSPHATE ChEMBL CHEMBL437508 DrugBank DB01717 ZINC ZINC000096085195 PDB chain 3dl0 Chain B Residue 218 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 3dl0 Effectiveness and limitations of local structural entropy optimization in the thermal stabilization of mesophilic and thermophilic adenylate kinases. Resolution 1.58 Å Binding residue (original residue number in PDB) P9 G10 G12 K13 G14 T15 T31 G32 F35 R36 E57 V59 T64 G85 R88 Q92 R123 R127 H138 F141 R160 R171 Q199 I201 Binding residue (residue number reindexed from 1) P9 G10 G12 K13 G14 T15 T31 G32 F35 R36 E57 V59 T64 G85 R88 Q92 R123 R127 H138 F141 R160 R171 Q199 I201 Annotation score 4

Enzymatic activity Catalytic site (original residue number in PDB) K13 R88 R127 R160 R171 Catalytic site (residue number reindexed from 1) K13 R88 R127 R160 R171 Enzyme Commision number 2.7.4.3: adenylate kinase.

Gene Ontology Molecular Function GO:0004017 adenylate kinase activity GO:0004550 nucleoside diphosphate kinase activity GO:0005524 ATP binding GO:0008270 zinc ion binding GO:0016301 kinase activity GO:0016776 phosphotransferase activity, phosphate group as acceptor GO:0019205 nucleobase-containing compound kinase activity GO:0046872 metal ion binding GO:0050145 nucleoside monophosphate kinase activity

	Biological Process
GO:0006139	nucleobase-containing compound metabolic process
GO:0009123	nucleoside monophosphate metabolic process
GO:0009132	nucleoside diphosphate metabolic process
GO:0009165	nucleotide biosynthetic process
GO:0016310	phosphorylation
GO:0044209	AMP salvage
GO:0046940	nucleoside monophosphate phosphorylation

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component