Structure of PDB 8fv7 Chain BBB Binding Site BS03

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 IDGTF
InChIInChI=1S/C9H14F2N3O13P3/c10-9(11)6(15)4(25-7(9)14-2-1-5(12)13-8(14)16)3-24-29(20,21)27-30(22,23)26-28(17,18)19/h1-2,4,6-7,15H,3H2,(H,20,21)(H,22,23)(H2,12,13,16)(H2,17,18,19)/t4-,6-,7-/m1/s1
InChIKeyYMOXEIOKAJSRQX-QPPQHZFASA-N
SMILES
SoftwareSMILES
CACTVS 3.385NC1=NC(=O)N(C=C1)[C@@H]2O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[C@@H](O)C2(F)F
ACDLabs 12.01FC2(F)C(N1C(=O)N=C(N)C=C1)OC(C2O)COP(OP(O)(=O)OP(O)(O)=O)(O)=O
OpenEye OEToolkits 2.0.6C1=CN(C(=O)N=C1N)[C@H]2C([C@@H]([C@H](O2)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)(F)F
OpenEye OEToolkits 2.0.6C1=CN(C(=O)N=C1N)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)(F)F
CACTVS 3.385NC1=NC(=O)N(C=C1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)C2(F)F
FormulaC9 H14 F2 N3 O13 P3
Name2'-deoxy-2',2'-difluorocytidine 5'-(tetrahydrogen triphosphate);
Gemcitabine-TRIPHOSPHATE
ChEMBLCHEMBL1201383
DrugBank
ZINCZINC000013546270
PDB chain8fv7 Chain BBB Residue 704 [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)		S14 D147 I148 E149
Binding residue
(residue number reindexed from 1)		S14 D147 I148 E149
Annotation score2
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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