Structure of PDB 2gks Chain B Binding Site BS01

Receptor Information
>2gks Chain B (length=529) Species: 63363 (Aquifex aeolicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIKYLKSIQISQRSVLDLELLAVGAFTPLDRFMGEEDYRNVVESMRLKSG
TLFPIPITLPMEKEIAKDLKEGEWIVLRDPKNVPLAIMRVEEVYKWNLEY
EAKNVLGTTDPRHPLVAEMHTWGEYYISGELKVIQLPKYYDFPEYRKTPK
QVREEIKSLGLDKIVAFQTRNPMHRVHEELTKRAMEKVGGGLLLHPVVGL
TKPGDVDVYTRMRIYKVLYEKYYDKKKTILAFLPLAMRMAGPREALWHGI
IRRNYGATHFIVGRDHASPGKDSKGKPFYDPYEAQELFKKYEDEIGIKMV
PFEELVYVPELDQYVEINEIRENFLKQGRKLPEWFTRPEVAEILAETYVP
KHKQGFCVWLTGLPCAGKSTIAEILATMLQARGRKVTLLDGDVVRTHLSR
GLGFSKEDRITNILRVGFVASEIVKHNGVVICALVSPYRSARNQVRNMME
EGKFIEVFVDAPVEVCEERDVKGLYKKAKEGLIKGFTGVDDPYEPPVAPE
VRVDTTKLTPEESALKILEFLKKEGFIKD
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=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)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain2gks Chain B Residue 906 [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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PDB2gks Crystal structure of the bifunctional ATP sulfurylase-APS kinase from the chemolithotrophic thermophile Aquifex aeolicus.
Resolution2.31 Å
Binding residue
(original residue number in PDB)		F169 Q170 T171 R172 N173 H179 L182 G265 R266 H268 A269 E306 L307
Binding residue
(residue number reindexed from 1)		F167 Q168 T169 R170 N171 H177 L180 G263 R264 H266 A267 E304 L305
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) T171 R172 H176 H179 R266
Catalytic site (residue number reindexed from 1) T169 R170 H174 H177 R264
Enzyme Commision number 2.7.1.25: adenylyl-sulfate kinase.
2.7.7.4: sulfate adenylyltransferase.
Gene Ontology
Molecular Function
GO:0004020 adenylylsulfate kinase activity
GO:0004781 sulfate adenylyltransferase (ATP) activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0000103 sulfate assimilation
GO:0006790 sulfur compound metabolic process
GO:0010134 sulfate assimilation via adenylyl sulfate reduction
GO:0016310 phosphorylation
GO:0019379 sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
GO:0070814 hydrogen sulfide biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2gks, PDBe:2gks, PDBj:2gks
PDBsum2gks
PubMed17095009
UniProtO67174|SATC_AQUAE Probable bifunctional SAT/APS kinase (Gene Name=sat/cysC)

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