Structure of PDB 1w78 Chain A

Receptor sequence
>1w78A (length=414) Species: 562 (Escherichia coli) [Search protein sequence]
TPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVA
GTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAH
TASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDA
TNIVDADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEM
PSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSDAHGTLENLPLPLVPQ
PNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAH
NPHAAEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCA
PLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLVCGSFH
TVAHVMEVIDARRS
3D structure
PDB1w78 Escherichia Coli Folc Structure Reveals an Unexpected Dihydrofolate Binding Site Providing an Attractive Target for Anti-Microbial Therapy
ChainA
Resolution1.82 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.2.12: dihydrofolate synthase.
6.3.2.17: tetrahydrofolate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004326 tetrahydrofolylpolyglutamate synthase activity
GO:0005524 ATP binding
GO:0008841 dihydrofolate synthase activity
GO:0016874 ligase activity
GO:0016881 acid-amino acid ligase activity
GO:0046872 metal ion binding
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0006761 dihydrofolate biosynthetic process
GO:0009058 biosynthetic process
GO:0009257 10-formyltetrahydrofolate biosynthetic process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
GO:0046901 tetrahydrofolylpolyglutamate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Cellular Component
External links
PDB RCSB:1w78, PDBe:1w78, PDBj:1w78
PDBsum1w78
PubMed15705579
UniProtP08192|FOLC_ECOLI Dihydrofolate synthase/folylpolyglutamate synthase (Gene Name=folC)

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