Structure of PDB 2fmt Chain B Binding Site BS02

Receptor Information
>2fmt Chain B (length=314) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSP
VKVLAEEKGLPVFQPVSLRPQENQQLVAELQADVMVVVAYGLILPKAVLE
MPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAETGVTIMQMDVGLDTGDM
LYKLSCPITAEDTSGTLYDKLAELGPQGLITTLKQLADGTAKPEVQDETL
VTYAEKLSKEEARIDWSLSAAQLERCIRAFNPWPMSWLEIEGQPVKVWKA
SVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDLL
NSRREWFVPGNRLV
Ligand information
Ligand IDFME
InChIInChI=1S/C6H11NO3S/c1-11-3-2-5(6(9)10)7-4-8/h4-5H,2-3H2,1H3,(H,7,8)(H,9,10)/t5-/m0/s1
InChIKeyPYUSHNKNPOHWEZ-YFKPBYRVSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CSCC[C@H](NC=O)C(O)=O
CACTVS 3.341CSCC[CH](NC=O)C(O)=O
ACDLabs 10.04O=CNC(C(=O)O)CCSC
OpenEye OEToolkits 1.5.0CSCCC(C(=O)O)NC=O
OpenEye OEToolkits 1.5.0CSCC[C@@H](C(=O)O)NC=O
FormulaC6 H11 N O3 S
NameN-FORMYLMETHIONINE
ChEMBL
DrugBankDB04464
ZINCZINC000001529464
PDB chain2fmt Chain D Residue 586 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2fmt Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		F14 A89 Y90 G119
Binding residue
(residue number reindexed from 1)		F14 A89 Y90 G119
Annotation score1
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2fmt, PDBe:2fmt, PDBj:2fmt
PDBsum2fmt
PubMed9843487
UniProtP23882|FMT_ECOLI Methionyl-tRNA formyltransferase (Gene Name=fmt)

[Back to BioLiP]