Structure of PDB 8fv7 Chain BBB Binding Site BS02

Receptor Information
>8fv7 Chain BBB (length=535) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPG
TMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKMSRRNNFTTGRIYSDVL
RKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIES
LPFLEAIRQMAVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLS
IGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVDSIYKIPGL
LKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIE
LPDAYKSVIEALKHGGLKNRVSVNIKLIDSQDVETRGVEILKGLDAILVP
GGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENAN
STEFVPDCKYPVVALITEWRDENGNVEVGTMRLGAQQCQLVDDSLVRQLY
NAPTIVERHRHRYEVNNMLLKQIEDAGLRVAGRSGDDQLVEIIEVPNHPW
FVACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQ
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 chain8fv7 Chain BBB Residue 703 [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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PDB8fv7 A metal-dependent conformational change provides a structural basis for the inhibition of CTP synthase by gemcitabine-5'-triphosphate.
Resolution2.08 Å
Binding residue
(original residue number in PDB)		S15 G17 K18 G19 I20 R211 D240 V241
Binding residue
(residue number reindexed from 1)		S15 G17 K18 G19 I20 R211 D240 V241
Annotation score5
Enzymatic activity
Enzyme Commision number 6.3.4.2: CTP synthase (glutamine hydrolyzing).
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003883 CTP synthase activity
GO:0004359 glutaminase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006241 CTP biosynthetic process
GO:0006541 glutamine metabolic process
GO:0019856 pyrimidine nucleobase biosynthetic process
GO:0044210 'de novo' CTP biosynthetic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex
GO:0097268 cytoophidium

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8fv7, PDBe:8fv7, PDBj:8fv7
PDBsum8fv7
PubMed37106216
UniProtP0A7E5|PYRG_ECOLI CTP synthase (Gene Name=pyrG)

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