Structure of PDB 1qdt Chain A

Receptor sequence
>1qdtA (length=312) Species: 562 (Escherichia coli) [Search protein sequence]
MVEPQHNVMQMGGDFANNPNAQQFIDKMVNKHGFDRQQLQEILSQAKRLD
SVLRLMDNQGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYG
VPPEIIVGIIGVETRWGRVMGKTRILDALATLSFNYPRRAEYFSGELETF
LLMARDEQDDPLNLKGSFAGAMGYGQFMPSSYKQYAVDFSGDGHINLWDP
VDAIGSVANYFKAHGWVKGDQVAVMANGQAPGLPNGFKTKYSISQLAAAG
LTPQQPLGNHQQASLLRLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVW
QLGQAVALARVQ
3D structure
PDB1qdt Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability.
ChainA
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1qdt, PDBe:1qdt, PDBj:1qdt
PDBsum1qdt
PubMed10570954
UniProtP41052|MLTB_ECOLI Membrane-bound lytic murein transglycosylase B (Gene Name=mltB)

[Back to BioLiP]