Structure of PDB 4lnk Chain A Binding Site BS05

Receptor Information
>4lnk Chain A (length=443) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKYTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVM
FDGSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDG
TPFEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELN
DKGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKY
AGAVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLF
KNGVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVP
GYEAPCYVAWSAQNRSPLIRIPASRGISTRVEVRSVDPAANPYLALSVLL
AAGLDGIKNKLEAPAPIDRNIYVMSKEERMENGIVDLPATLAEALEEFKS
NEVMVKALGEHLFEHFIEAKEIEWDMFRTQVHPWEREQYMSQY
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 chain4lnk Chain F Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4lnk Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism.
Resolution2.87 Å
Binding residue
(original residue number in PDB)		K44 M51
Binding residue
(residue number reindexed from 1)		K43 M50
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D53 E132 E134 E189 E196 H245 R316 E333 R335
Catalytic site (residue number reindexed from 1) D52 E131 E133 E188 E195 H244 R315 E332 R334
Enzyme Commision number 6.3.1.2: glutamine synthetase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016595 glutamate binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
GO:0070406 glutamine binding
GO:0140297 DNA-binding transcription factor binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0043562 cellular response to nitrogen levels
GO:0045892 negative regulation of DNA-templated transcription
GO:0090295 nitrogen catabolite repression of transcription
GO:1904797 negative regulation of core promoter binding
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:4lnk, PDBe:4lnk, PDBj:4lnk
PDBsum4lnk
PubMed24158439
UniProtP12425|GLN1A_BACSU Glutamine synthetase (Gene Name=glnA)

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