Structure of PDB 4ii9 Chain A Binding Site BS02
Receptor Information
>4ii9 Chain A (length=337) Species:
1629
(Weissella viridescens) [
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PVLNLNDPQAVERYEEFMRQSPYGQVTQDLGWAKVKNNWEPVDVYLEDDQ
GAIIAAMSMLLGDTPTDKKFAYASKGPVMDVTDVDLLDRLVDEAVKALDG
RAYVLRFDPEVAYSDEFNTTLQDHGYVTRNRNVADAGMHATIQPRLNMVL
DLTKFPDAKTTLDLYPSKTKSKIKRPFRDGVEVHSGNSATELDEFFKTYT
TMAERHGITHRPIEYFQRMQAAFDADTMRIFVAEREGKLLSTGIALKYGR
KIWYMYAGSMDGNTYYAPYAVQSEMIQWALDTNTDLYDLGGIESESTDDS
LYVFKHVFVKDAPREYIGEIDKVLDPEVYAELVKDGH
Ligand information
>4ii9 Chain C (length=3) [
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cca
...
Receptor-Ligand Complex Structure
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PDB
4ii9
The Structure of FemXWv in Complex with a Peptidyl-RNA Conjugate: Mechanism of Aminoacyl Transfer from Ala-tRNA(Ala) to Peptidoglycan Precursors
Resolution
1.66 Å
Binding residue
(original residue number in PDB)
M202 H206 A257 S259 P268 G291 S300 K305
Binding residue
(residue number reindexed from 1)
M202 H206 A257 S259 P268 G291 S300 K305
Enzymatic activity
Catalytic site (original residue number in PDB)
K36 D108 R211 F304 K305 E319
Catalytic site (residue number reindexed from 1)
K36 D108 R211 F304 K305 E319
Enzyme Commision number
2.3.2.10
: UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase.
Gene Ontology
Molecular Function
GO:0016746
acyltransferase activity
GO:0016755
aminoacyltransferase activity
GO:0047206
UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase activity
Biological Process
GO:0008360
regulation of cell shape
GO:0009252
peptidoglycan biosynthetic process
GO:0044038
cell wall macromolecule biosynthetic process
GO:0071555
cell wall organization
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Molecular Function
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Biological Process
External links
PDB
RCSB:4ii9
,
PDBe:4ii9
,
PDBj:4ii9
PDBsum
4ii9
PubMed
23744707
UniProt
Q9EY50
|FEMX_WEIVI UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase (Gene Name=femX)
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