Structure of PDB 6fv4 Chain A

Receptor sequence
>6fv4A (length=381) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
GSHMLLTADTVLTGTELLRPGWLEIASDRVVAVGAGAPPAQADRNLGAAT
VVPGFVDTHLHGGGGGNFSAATDDETARAVALHRAHGSTTLVASLVTAGP
EDLLRQVSGLARQVRAGLIDGIHLEGPWLSTLRCGAHQPVLMRDPDPGEI
GRVLDAGEGTVRMVTIAPERDGALAAIAQLVNAGVVAAVGHTEATYDQTR
AAIDAGATVGTHLFNAMRPIDRREPGPAVALTEDSRVTVEMIVDGVHVAP
AIYRHITQTVGPERLSLITAAMAATGMSDGVYRLGPLDIDVVAGVARVAG
TDTIAGSTATMEQVFRLAVAHCGLPRDDALSLAVRQACVNPARALGLPAA
GLAAGARADLVVLDHDLAVTAVMRAGEWVVT
3D structure
PDB6fv4 Structural and functional determination of homologs of theMycobacterium tuberculosis N-acetylglucosamine-6-phosphate deacetylase (NagA).
ChainA
Resolution1.974 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 A H56 H58 E122 H59 H61 E125
BS02 16G A G132 A133 H134 H188 N212 A213 H244 I301 A302 G303 G135 A136 H137 H191 N215 A216 H247 I304 A305 G306 PDBbind-CN: -logKd/Ki=2.92,Kd=1.2mM
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:6fv4, PDBe:6fv4, PDBj:6fv4
PDBsum6fv4
PubMed29728457
UniProtA0QU89

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