Structure of PDB 7rmv Chain E Binding Site BS01

Receptor Information
>7rmv Chain E (length=553) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKYVVVSGGVISGIGKGVLASSTGMLMKTLGLKVTSIKIDPYMNIDAGTM
SPLEHGECFVLDDGGETDLDLGNYERYLGVTLTKDHNITTGKIYSHVIAK
ERKGDYLGKTVQIVPHLTNAIQDWIERVAKIPVDDTGMEPDVCIIELGGT
VGDIESAPFVEALRQFQFKVGKENFALIHVSLVPVIHGEQKTKPTQAAIK
GLRSLGLVPDMIACRCSETLDKPTIDKIAMFCHVGPEQVVNVHDVNSTYH
VPLLLLEQKMIDYLHARLKLDEISLTEEEELLSKWKATTGNFDETVKIAL
VGKYTNLKDSYLSVIKALEHSSMKCRRKLDIKWVEATDLEPEAQESNKTK
FREAWNMVSTADGILIPGGFGVRGTEGMVLAARWARENHIPFLGVCLGLQ
IATIEFTRSVLGRKDSHSAEFYPDIDEKNHVVVFMMRLGLRPTFFQNETE
WSQIKKLYGDVSEVHERHRHRYEINPKMVDELENNGLIFVGKDDTGKRCE
ILELKNHPYYIATQYHPEYTSKVLDPSKPFLGLVAASAGILQDVIEGKYD
LEA
Ligand information
Ligand IDUTP
InChIInChI=1S/C9H15N2O15P3/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(24-8)3-23-28(19,20)26-29(21,22)25-27(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,21,22)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
InChIKeyPGAVKCOVUIYSFO-XVFCMESISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)O[P@@](=O)(O)OP(=O)(O)O)O)O
CACTVS 3.341O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O
OpenEye OEToolkits 1.5.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O
CACTVS 3.341O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P@](O)(=O)O[P@](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
FormulaC9 H15 N2 O15 P3
NameURIDINE 5'-TRIPHOSPHATE
ChEMBLCHEMBL336296
DrugBankDB04005
ZINCZINC000003861755
PDB chain7rmv Chain E Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7rmv Cryo-EM structures of CTP synthase filaments reveal mechanism of pH-sensitive assembly during budding yeast starvation.
Resolution6.7 Å
Binding residue
(original residue number in PDB)
Q190 K191 T192 K193
Binding residue
(residue number reindexed from 1)
Q190 K191 T192 K193
Annotation score4
Enzymatic activity
Enzyme Commision number 6.3.4.2: CTP synthase (glutamine hydrolyzing).
Gene Ontology
Molecular Function
GO:0003883 CTP synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042802 identical protein binding
Biological Process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006241 CTP biosynthetic process
GO:0006541 glutamine metabolic process
GO:0008654 phospholipid biosynthetic process
GO:0019856 pyrimidine nucleobase biosynthetic process
GO:0044210 'de novo' CTP biosynthetic process
Cellular Component
GO:0000324 fungal-type vacuole
GO:0005737 cytoplasm
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:7rmv, PDBe:7rmv, PDBj:7rmv
PDBsum7rmv
PubMed34734801
UniProtP28274|URA7_YEAST CTP synthase 1 (Gene Name=URA7)

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