Structure of PDB 4cfp Chain A

Receptor sequence
>4cfpA (length=327) Species: 562 (Escherichia coli) [Search protein sequence]
DTNGFDILMGQFAHNIENIWGFKEVVIAGPKDYVKYTDQYQTRSHINFDD
GTITIETIAGTEPAAHLRRAIIKTLLMGDDPSSVDLYSDVDDITISKEPF
LYGQVVDNTGQPIRWEGRASNFADYLLKNRLKSRSNGLRIIYSVTINMVP
NHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTQSSFNPYAVSRSDALG
LMQVVQHTAGKDVFRSQGKSGTPSRSFLFDPASNIDTGTAYLAMLNNVYL
GGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMTPGDVYQT
LTTRHPSAESRRYLYKVNTAQKSYRRR
3D structure
PDB4cfp Structure and Cell Wall Cleavage by Modular Lytic Transglycosylase Mltc of Escherichia Coli.
ChainA
Resolution2.15 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.2.n1: peptidoglycan lytic exotransglycosylase.
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 AMV A Q217 S226 R227 S228 Q235 Y299 E341 Q185 S194 R195 S196 Q203 Y267 E309
BS02 AMU A T240 D244 Y273 G301 G302 G304 R308 T208 D212 Y241 G269 G270 G272 R276
Gene Ontology
Molecular Function
GO:0008932 lytic endotransglycosylase activity
GO:0008933 lytic transglycosylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016829 lyase activity
Biological Process
GO:0009253 peptidoglycan catabolic process
GO:0016998 cell wall macromolecule catabolic process
GO:0034599 cellular response to oxidative stress
GO:0051301 cell division
GO:0071236 cellular response to antibiotic
GO:0071555 cell wall organization
Cellular Component
GO:0009279 cell outer membrane
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4cfp, PDBe:4cfp, PDBj:4cfp
PDBsum4cfp
PubMed24988330
UniProtP0C066|MLTC_ECOLI Membrane-bound lytic murein transglycosylase C (Gene Name=mltC)

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