Structure of PDB 2fmt Chain A Binding Site BS01
Receptor Information
>2fmt Chain A (length=314) Species:
562
(Escherichia coli) [
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SESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSP
VKVLAEEKGLPVFQPVSLRPQENQQLVAELQADVMVVVAYGLILPKAVLE
MPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAETGVTIMQMDVGLDTGDM
LYKLSCPITAEDTSGTLYDKLAELGPQGLITTLKQLADGTAKPEVQDETL
VTYAEKLSKEEARIDWSLSAAQLERCIRAFNPWPMSWLEIEGQPVKVWKA
SVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDLL
NSRREWFVPGNRLV
Ligand information
>2fmt Chain C (length=77) [
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cgcgggguggagcagccugguagcucgucgggcucauaacccgaagaucg
ucgguucaaauccggcccccgcaacca
.<<<<<<..<<<<.........>>>>.<<<<<.......>>>>>.....<
<<<<.......>>>>>>>>>>>.....
Receptor-Ligand Complex Structure
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PDB
2fmt
Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
T11 P12 P39 A40 G41 R42 G43 K44 A89 G91 K206 L207 K209 W233 K246 A289 G290 K291 M294 D298 N301 S302 R304
Binding residue
(residue number reindexed from 1)
T11 P12 P39 A40 G41 R42 G43 K44 A89 G91 K206 L207 K209 W233 K246 A289 G290 K291 M294 D298 N301 S302 R304
Enzymatic activity
Enzyme Commision number
2.1.2.9
: methionyl-tRNA formyltransferase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004479
methionyl-tRNA formyltransferase activity
GO:0016740
transferase activity
Biological Process
GO:0006412
translation
GO:0006413
translational initiation
GO:0009058
biosynthetic process
GO:0019988
charged-tRNA amino acid modification
GO:0071951
conversion of methionyl-tRNA to N-formyl-methionyl-tRNA
Cellular Component
GO:0005829
cytosol
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Molecular Function
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Cellular Component
External links
PDB
RCSB:2fmt
,
PDBe:2fmt
,
PDBj:2fmt
PDBsum
2fmt
PubMed
9843487
UniProt
P23882
|FMT_ECOLI Methionyl-tRNA formyltransferase (Gene Name=fmt)
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