Structure of PDB 3qbw Chain B

Receptor sequence
>3qbwB (length=356) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
PRYLGLMSGTSLDGMDIVLIEQGDRTTLLASHYLPMPAGLREDILALCVP
GPDEIARAAEVEQRWVALAAQGVRELLLQQQMSPDEVRAIGSHGQTIRHE
PARHFTVQIGNPALLAELTGIDVVADFRRRDVAAGGQGAPLVPAFHQALF
GTSRAVLNIGGFSNVSLLSPGKPVRGFDCGPGNVLMDAWIHHQRGEHFDR
DGAWAASGQVNHALLASLLADEFFAARGPKSTGRERFNLPWLQEHLALPA
ADIQATLLELSARSISESLLDAQPDCEEVLVCGGGAFNTALMKRLAMLMP
EARVASTDEYGIPPAWMEGMAFAWLAHRFLERLPGNCPDVTGALGPRTLG
ALYPAG
3D structure
PDB3qbw Molecular Basis of 1,6-Anhydro Bond Cleavage and Phosphoryl Transfer by Pseudomonas aeruginosa 1,6-Anhydro-N-acetylmuramic Acid Kinase.
ChainB
Resolution2.23 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.1.170: anhydro-N-acetylmuramic acid kinase.
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 ADP B G10 S12 D14 N187 D191 F202 D205 G291 G292 F295 N296 G9 S11 D13 N183 D187 F198 D201 G283 G284 F287 N288
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
Biological Process
GO:0006040 amino sugar metabolic process
GO:0009254 peptidoglycan turnover
GO:0016310 phosphorylation
GO:0046677 response to antibiotic
GO:0097175 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3qbw, PDBe:3qbw, PDBj:3qbw
PDBsum3qbw
PubMed21288904
UniProtQ9I5Q5|ANMK_PSEAE Anhydro-N-acetylmuramic acid kinase (Gene Name=anmK)

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