Structure of PDB 4chx Chain A Binding Site BS01

Receptor Information
>4chx Chain A (length=327) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DTNGFDILMGQFAHNIENIWGFKEVVIAGPKDYVKYTDQYQTRSHINFDD
GTITIETIAGTEPAAHLRRAIIKTLLMGDDPSSVDLYSDVDDITISKEPF
LYGQVVDNTGQPIRWEGRASNFADYLLKNRLKSRSNGLRIIYSVTINMVP
NHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTQSSFNPYAVSRSDALG
LMQVVQHTAGKDVFRSQGKSGTPSRSFLFDPASNIDTGTAYLAMLNNVYL
GGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMTPGDVYQT
LTTRHPSAESRRYLYKVNTAQKSYRRR
Ligand information
Receptor-Ligand Complex Structure
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PDB4chx Structure and Cell Wall Cleavage by Modular Lytic Transglycosylase Mltc of Escherichia Coli.
Resolution2.45 Å
Binding residue
(original residue number in PDB)
F37 D38 M41 G42 I59 A60 G61 P62
Binding residue
(residue number reindexed from 1)
F5 D6 M9 G10 I27 A28 G29 P30
Enzymatic activity
Enzyme Commision number 4.2.2.n1: peptidoglycan lytic exotransglycosylase.
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:4chx, PDBe:4chx, PDBj:4chx
PDBsum4chx
PubMed24988330
UniProtP0C066|MLTC_ECOLI Membrane-bound lytic murein transglycosylase C (Gene Name=mltC)

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