Structure of PDB 2fmt Chain A

Receptor sequence
>2fmtA (length=314) Species: 562 (Escherichia coli) [Search protein sequence]
SESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSP
VKVLAEEKGLPVFQPVSLRPQENQQLVAELQADVMVVVAYGLILPKAVLE
MPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAETGVTIMQMDVGLDTGDM
LYKLSCPITAEDTSGTLYDKLAELGPQGLITTLKQLADGTAKPEVQDETL
VTYAEKLSKEEARIDWSLSAAQLERCIRAFNPWPMSWLEIEGQPVKVWKA
SVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDLL
NSRREWFVPGNRLV
3D structure
PDB2fmt Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.
ChainA
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.2.9: methionyl-tRNA formyltransferase.
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 rna A T11 P12 P39 A40 G41 R42 G43 K44 A89 G91 K206 L207 K209 W233 K246 A289 G290 K291 M294 D298 N301 S302 R304 T11 P12 P39 A40 G41 R42 G43 K44 A89 G91 K206 L207 K209 W233 K246 A289 G290 K291 M294 D298 N301 S302 R304
BS02 FME A F14 A89 Y90 G119 F14 A89 Y90 G119
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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Cellular Component
External links
PDB RCSB:2fmt, PDBe:2fmt, PDBj:2fmt
PDBsum2fmt
PubMed9843487
UniProtP23882|FMT_ECOLI Methionyl-tRNA formyltransferase (Gene Name=fmt)

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