Structure of PDB 1yrr Chain A

Receptor sequence

>1yrrA (length=381) Species: 562 (Escherichia coli)

MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAI
LSPGFIDVQLNGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLI
TTSDELMKQGVRVMREYLAKHPNQALGLHLEGPWLNLVKKTHNPNFVRKP
DAALVDFLCENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLK
EAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEADIYCGIIADGLH
VDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVD
ENGTLSGSSLTMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGT
LAAGKVANLTAFTPDFKITKTIVNGNEVVTQ

3D structure

• PDB: 1yrr Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Enzyme Commision number: 3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase.

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	PO4	A	E131 H195 H216 D273	E131 H194 H215 D272

Gene Ontology

Molecular Function

• GO:0008270 zinc ion binding
• GO:0008448 N-acetylglucosamine-6-phosphate deacetylase activity
• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding
• GO:0047419 N-acetylgalactosamine-6-phosphate deacetylase activity

Biological Process

• GO:0006040 amino sugar metabolic process
• GO:0006044 N-acetylglucosamine metabolic process
• GO:0006046 N-acetylglucosamine catabolic process
• GO:0019262 N-acetylneuraminate catabolic process
• GO:0051289 protein homotetramerization

Cellular Component

• GO:0032991 protein-containing complex

External links

• PDB: RCSB:1yrr, PDBe:1yrr, PDBj:1yrr
• PDBsum: 1yrr
• PubMed: 16630633
• UniProt: P0AF18|NAGA_ECOLI N-acetylglucosamine-6-phosphate deacetylase (Gene Name=nagA)