Structure of PDB 8ooz Chain I Binding Site BS01

Receptor Information
>8ooz Chain I (length=429) Species: 1122233 (Methermicoccus shengliensis DSM 18856) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SKEDEIFRIVEEKNVRFVRLQFVDVQGIPKNVAIPVGQLEKALGPGIHFD
GSSDMVLRPDPDTFRVLPWSGNGTAEARLICDIELPDGKPFMGCPRQVLK
KNMEEAAKLGYVMNTGPEMEFFLFKRQDGMPTNIPQDRGGYFDLAPIDLA
EEIKREIVLVLEEMGFEVEAAHHEVAFGQHEIDFKYDNALATADNVITLK
YVAKTLALQHGLHATFMPKPIFGVNGSGMHTNTSLFKDGKNAFYDPDAPD
QISDTLRYFVGGVLKHIRAITAITNPLVNSYKRLVPGYEAPVYITWSGPN
RSSLIRVPAPRGNSTRIEIRSPDPSCNPYLAFAAILAAGLDGVKNKIEPP
ERVEKNIYKLTEEEREKLGIGMLPGTLKEAIECFKEDELLVSALGEHVSQ
SIINVAMADWDSYRTQVHQWELDRYLQTY
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 chain8ooz Chain I Residue 501 [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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PDB8ooz Differences in the regulation mechanisms of the glutamine synthetase from methanogenic archaea unveiled by structural investigations.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		E182 F197 K198 Y199 N245 S247 S327 R329
Binding residue
(residue number reindexed from 1)		E169 F184 K185 Y186 N232 S234 S314 R316
Annotation score5
Enzymatic activity
Enzyme Commision number 6.3.1.2: glutamine synthetase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8ooz, PDBe:8ooz, PDBj:8ooz
PDBsum8ooz
PubMed38243071
UniProtA0A832VZP6

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