Structure of PDB 1fpm Chain A

Receptor sequence
>1fpmA (length=549) Species: 1525 (Moorella thermoacetica) [Search protein sequence]
DIEIAQAAKMKPVMELARGLGIQEDEVELYGKYKAKISLDVYRRLKDKPD
GKLILVTAITPTPAGEGKTTTSVGLTDALARLGKRVMVCLREPSLGPSFG
IKGGAAGGGYAQVVPMEDINLHFTGDIHAVTYAHNLLAAMVDNHLQQGNV
LNIDPRTITWRRVIDLNDRALRNIVIGLGGKANGVPRETGFDISVASEVM
ACLCLASDLMDLKERFSRIVVGYTYDGKPVTAGDLEAQGSMALLMKDAIK
PNLVQTLENTPAFIHGGPFANIAHGCNSIIATKTALKLADYVVTEAGFGA
DLGAEKFYDVKCRYAGFKPDATVIVATVRALKMHGGVPKSDLATENLEAL
REGFANLEKHIENIGKFGVPAVVAINAFPTDTEAELNLLYELCAKAGAEV
ALSWAKGGEGGLELARKVLQTLESRPSNFHVLYNLDLSIKDKIAKIATEI
YGADGVNYTAEADKAIQRYESLGYGNLPVVMAKTQYSFSDDMTKLGRPRN
FTITVREVRLSAGGRLIVPITGAIMTMPGLPKRPAACNIDIDADGVITG
3D structure
PDB1fpm Cation binding and thermostability of FTHFS monovalent cation binding sites and thermostability of N10-formyltetrahydrofolate synthetase from Moorella thermoacetica.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K74 T76 R97 K108 A276 F304 F384 W412
Catalytic site (residue number reindexed from 1) K68 T70 R91 K102 A270 F298 F378 W404
Enzyme Commision number 6.3.4.3: formate--tetrahydrofolate ligase.
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 CS A E98 N126 L127 E92 N120 L121
Gene Ontology
Molecular Function
GO:0004329 formate-tetrahydrofolate ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006730 one-carbon metabolic process
GO:0035999 tetrahydrofolate interconversion

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Molecular Function

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Biological Process
External links
PDB RCSB:1fpm, PDBe:1fpm, PDBj:1fpm
PDBsum1fpm
PubMed11087401
UniProtP21164|FTHS_MOOTH Formate--tetrahydrofolate ligase (Gene Name=fhs)

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