Structure of PDB 5u3c Chain A

Receptor sequence
>5u3cA (length=534) Species: 562 (Escherichia coli) [Search protein sequence]
MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPG
TMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKMSRRNNFTTGRIYSDVL
RKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIES
LPFLEAIRQMAVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLS
IGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVDSIYKIPGL
LKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIE
LPDAYKSVIEALKHGGLKNRVSVNIKLIDSQDVETRGVEILKGLDAILVP
GGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENAN
STEFVPDCKYPVVALITEWRDENGNVETMRLGAQQCQLVDDSLVRQLYNA
PTIVERHRHRYEVNNMLLKQIEDAGLRVAGRSGDDQLVEIIEVPNHPWFV
ACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQA
3D structure
PDB5u3c Human CTP synthase filament structure reveals the active enzyme conformation.
ChainA
Resolution4.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.4.2: CTP synthase (glutamine hydrolyzing).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CTP A D147 I148 E149 D147 I148 E149
BS02 ADP A G17 I20 R211 D240 V241 G17 I20 R211 D240 V241
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:5u3c, PDBe:5u3c, PDBj:5u3c
PDBsum5u3c
PubMed28459447
UniProtP0A7E5|PYRG_ECOLI CTP synthase (Gene Name=pyrG)

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