Structure of PDB 4cfo Chain B

Receptor sequence

>4cfoB (length=327) Species: 562 (Escherichia coli)

DTNGFDILMGQFAHNIENIWGFKEVVIAGPKDYVKYTDQYQTRSHINFDD
GTITIETIAGTEPAAHLRRAIIKTLLMGDDPSSVDLYSDVDDITISKEPF
LYGQVVDNTGQPIRWEGRASNFADYLLKNRLKSRSNGLRIIYSVTINMVP
NHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTQSSFNPYAVSRSDALG
LMQVVQHTAGKDVFRSQGKSGTPSRSFLFDPASNIDTGTAYLAMLNNVYL
GGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMTPGDVYQT
LTTRHPSAESRRYLYKVNTAQKSYRRR

3D structure

• PDB: 4cfo Structure and Cell Wall Cleavage by Modular Lytic Transglycosylase Mltc of Escherichia Coli.
• Chain: B
• Resolution: 2.9 Å

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	NM9	B	Q217 S226 S228 Q235 Y299 N300	Q185 S194 S196 Q203 Y267 N268
BS02	NM6	B	T240 D244 Y273 G302	T208 D212 Y241 G270

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

External links

• PDB: RCSB:4cfo, PDBe:4cfo, PDBj:4cfo
• PDBsum: 4cfo
• PubMed: 24988330
• UniProt: P0C066|MLTC_ECOLI Membrane-bound lytic murein transglycosylase C (Gene Name=mltC)