Structure of PDB 1d0l Chain A

Receptor sequence
>1d0lA (length=314) Species: 562 (Escherichia coli) [Search protein sequence]
MVEPQHNVMQMGGDFANNPNAQQFIDKMVNKHGFDRQQLQEILSQAKRLD
SVLRLMDNQAPGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALNRAWQV
YGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFNYPRRAEYFSGELE
TFLLMARDEQDDPLNLKGSFAGAMGYGQFMPSSYKQYAVDFSGDGHINLW
DPVDAIGSVANYFKAHGWVKGDQVAVMANGQAPGLPNGFKTKYSISQLAA
AGLTPQQPLGNHQQASLLRLDVGTGYQYWYGLPNFYTITRYNHSTHYAMA
VWQLGQAVALARVQ
3D structure
PDB1d0l Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan.
ChainA
Resolution1.97 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 D190 S192 D194 H196 D204
BS02 BLG A E162 Y191 S216 A218 Q225 F226 M227 S230 Y259 Y338 N339 H340 E115 Y144 S169 A171 Q178 F179 M180 S183 Y212 Y291 N292 H293
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:1d0l, PDBe:1d0l, PDBj:1d0l
PDBsum1d0l
PubMed10684641
UniProtP41052|MLTB_ECOLI Membrane-bound lytic murein transglycosylase B (Gene Name=mltB)

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