Structure of PDB 6fv3 Chain A

Receptor sequence
>6fv3A (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).
ChainA
Resolution2.58 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A H56 H58 E122 D267 H57 H59 E123 D268
BS02 ZN A 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

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

[Back to BioLiP]