Structure of PDB 4chx Chain A

Receptor sequence
>4chxA (length=327) Species: 562 (Escherichia coli) [Search protein sequence]
DTNGFDILMGQFAHNIENIWGFKEVVIAGPKDYVKYTDQYQTRSHINFDD
GTITIETIAGTEPAAHLRRAIIKTLLMGDDPSSVDLYSDVDDITISKEPF
LYGQVVDNTGQPIRWEGRASNFADYLLKNRLKSRSNGLRIIYSVTINMVP
NHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTQSSFNPYAVSRSDALG
LMQVVQHTAGKDVFRSQGKSGTPSRSFLFDPASNIDTGTAYLAMLNNVYL
GGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMTPGDVYQT
LTTRHPSAESRRYLYKVNTAQKSYRRR
3D structure
PDB4chx Structure and Cell Wall Cleavage by Modular Lytic Transglycosylase Mltc of Escherichia Coli.
ChainA
Resolution2.45 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 peptide A F37 D38 M41 G42 I59 A60 G61 P62 F5 D6 M9 G10 I27 A28 G29 P30
BS02 AH0 A P62 S226 R227 S228 E341 P30 S194 R195 S196 E309
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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