Structure of PDB 2oxn Chain A

Receptor sequence
>2oxnA (length=333) Species: 666 (Vibrio cholerae) [Search protein sequence]
MGPLWLDVAGYELSAEDREILQHPTVGGVILFGRNYHDNQQLLALNKAIR
QAAKRPILIGVDQEGGRVQRFREGFSRIPPAQYYARAENGVELAEQGGWL
MAAELIAHDVDLSFAPVLDMGFACKAIGNRAFGEDVQTVLKHSSAFLRGM
KAVGMATTGKHFPGHGAVIADSHLETPYDERETIAQDMAIFRAQIEAGVL
DAMMPAHVVYPHYDAQPASGSSYWLKQVLREELGFKGIVFSDDLSMEGAA
VMGGPVERSHQALVAGCDMILICNKREAAVEVLDNLPIMEVPQAEALLKK
QQFSYSELKRLERWQQASANMQRLIEQFSEHHH
3D structure
PDB2oxn Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance.
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
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 OAN A I30 D62 R130 K160 H161 M204 M246 I30 D62 R130 K160 H161 M204 M246 MOAD: Ki=0.036uM
PDBbind-CN: -logKd/Ki=7.44,Ki=36nM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0009254 peptidoglycan turnover
GO:0046677 response to antibiotic
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2oxn, PDBe:2oxn, PDBj:2oxn
PDBsum2oxn
PubMed17439950
UniProtQ9KU37|NAGZ_VIBCH Beta-hexosaminidase (Gene Name=nagZ)

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