Structure of PDB 1d0m Chain A

Receptor sequence
>1d0mA (length=312) Species: 562 (Escherichia coli) [Search protein sequence]
MVEPQHNVMQMGGDFANNPNAQQFIDKMVNKHGFDRQQLQEILSQAKRLD
SVLRLMDNQGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYG
VPPEIIVGIIGVETRWGRVMGKTRILDALATLSFNYPRRAEYFSGELETF
LLMARDEQDDPLNLKGSFAGAMGYGQFMPSSYKQYAVDFSGDGHINLWDP
VDAIGSVANYFKAHGWVKGDQVAVMANGQAPGLPNGFKTKYSISQLAAAG
LTPQQPLGNHQQASLLRLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVW
QLGQAVALARVQ
3D structure
PDB1d0m Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan.
ChainA
Resolution2.47 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 CA A D237 S239 D241 H243 D251 D188 S190 D192 H194 D202
BS02 BLG A E162 Y191 S216 F217 A218 Q225 M227 S230 Y259 Y338 H340 E113 Y142 S167 F168 A169 Q176 M178 S181 Y210 Y289 H291
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008932 lytic endotransglycosylase activity
GO:0008933 lytic transglycosylase activity
GO:0016829 lyase activity
GO:0031402 sodium ion binding
Biological Process
GO:0009253 peptidoglycan catabolic process
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:1d0m, PDBe:1d0m, PDBj:1d0m
PDBsum1d0m
PubMed10684641
UniProtP41052|MLTB_ECOLI Membrane-bound lytic murein transglycosylase B (Gene Name=mltB)

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