Structure of PDB 2p50 Chain B

Receptor sequence

>2p50B (length=356) Species: 83333 (Escherichia coli K-12)

MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAI
LSPGFIDVQLNGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLI
TTSDELMKQGVRVMREYLAKHPNQALGLHLEGPWLNLVKKGTHNPNFVRK
PDAALVDFLCENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATL
KEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEADIYCGIIADGL
HVDYANIRNAKRLKGDKLCLVTDATAPAGASGSSLTMIEGVRNLVEHCGI
ALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTAFTPDFKITKTIVNG
NEVVTQ

3D structure

• PDB: 2p50 Structural Diversity within the Mononuclear and Binuclear Active Sites of N-Acetyl-d-glucosamine-6-phosphate Deacetylase.
• Chain: B
• Resolution: 2.2 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	ZN	B	E131 H195 H216	E131 H195 H216

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:2p50, PDBe:2p50, PDBj:2p50
• PDBsum: 2p50
• PubMed: 17567048
• UniProt: P0AF18|NAGA_ECOLI N-acetylglucosamine-6-phosphate deacetylase (Gene Name=nagA)