Structure of PDB 6jku Chain B

Receptor sequence
>6jkuB (length=385) Species: 747 (Pasteurella multocida) [Search protein sequence]
LYKKAGFMYAFVNAVIYTAKDVLYGKALVVDGDKISAILPVEDVPENLQK
IDLQGNNLTAGFIDLQLNGCGGVMFNEDISVKTLEIMQETNLKSGTTSYL
PTFITSPDEGMKDAVKVMREYLTQYKNQALGLHFEGPYLSVEKKGVHREE
YIRAISPEMKTFLCDNADVITKITLAAENPTAQYIPDFVEKGIIVSLGHS
NATYDVAQQAIEKGASFATHLHNAMSPISSGRAMGVVGAVLDSDIYTGII
VDGLHVDYGNIRLDKKVKGDKLCIVTDATAAAGADIDSFVFVGKTVYVRD
GKCYDSNGTLGGAAITMIESVKNAVQEVGIPLDETLRMCNYYPAKAIGVD
HKLGSIEVGKIANLTAFTNDFNVLGTAVNGEWKAN
3D structure
PDB6jku Quaternary variations in the structural assembly of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella multocida.
ChainB
Resolution1.95 Å
3D
structure
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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 E128 H192 H213 E135 H199 H220
BS02 PO4 B E128 H192 D270 E135 H199 D277
BS03 PO4 B D298 N300 T302 D305 N307 T309
BS04 PO4 B D26 K27 K119 D33 K34 K126
Gene Ontology
Molecular Function
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:0046872 metal ion binding
Biological Process
GO:0006040 amino sugar metabolic process
GO:0006044 N-acetylglucosamine metabolic process
GO:0006046 N-acetylglucosamine catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6jku, PDBe:6jku, PDBj:6jku
PDBsum6jku
PubMed32865821
UniProtQ9CMF5

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