Structure of PDB 6fv3 Chain B

Receptor sequence
>6fv3B (length=378) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
HMLLTADTVLTGTELLRPGWLEIASDRVVAVGAGAPPAQADRNLGAATVV
PGFVDTHLHGGGGGNFSAATDDETARAVALHRAHGSTTLVASLVTAGPED
LLRQVSGLARQVRAGLIDGIHLEGPWLSTLRCGAHQPVLMRDPDPGEIGR
VLDAGEGTVRMVTIAPERDGALAAIAQLVNAGVVAAVGHTEATYDQTRAA
IDAGATVGTHLFNAMRPIDRREPGPAVALTEDSRVTVEMIVDGVHVAPAI
YRHITQTVGPERLSLITDAMAATGMSDGVYRLGPLDIDVVAGVARVAGTD
TIAGSTATMEQVFRLAVAHCGLPRDDALSLAVRQACVNPARALGLPAAGL
AAGARADLVVLDHDLAVTAVMRAGEWVV
3D structure
PDB6fv3 Structural and functional determination of homologs of theMycobacterium tuberculosis N-acetylglucosamine-6-phosphate deacetylase (NagA).
ChainB
Resolution2.58 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 H56 H58 E122 D267 H57 H59 E123 D268
BS02 ZN B E122 H188 H209 E123 H189 H210
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
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6fv3, PDBe:6fv3, PDBj:6fv3
PDBsum6fv3
PubMed29728457
UniProtA0QU89

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