Structure of PDB 3gsm Chain A

Receptor sequence
>3gsmA (length=324) Species: 666 (Vibrio cholerae) [Search protein sequence]
MGPLWLDVAGYELSAEDRAILAHPTVGGVILFGRNYHDNQQLLALNKAIR
QAAARPILIGVDQEGGRVQRFREGFSRIPPAQYYARAENGVELAEQGGWL
MAAELIAHDVDLSFAPVLDMGFACKAIGNRAFGEDVQTVLKHSSAFLRGM
KAVGMATTGKHFPGHGAVIADHLETPYDERETIAQDMAIFRAQIEAGVLD
AMMPAHVVYPHYDAQPASGSSYWLKQVLREELGFKGIVFSDDLSMVMGGP
VERSHQALVAGCDMILICNKREAAVEVLDNLPIMEVPQAEALLKKQQFSY
SELKRLERWQQASANMQRLIEQFS
3D structure
PDB3gsm Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ.
ChainA
Resolution2.4 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 VPU A D62 R130 K160 H161 M204 D62 R130 K160 H161 M203 PDBbind-CN: -logKd/Ki=6.48,Ki=0.33uM
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:3gsm, PDBe:3gsm, PDBj:3gsm
PDBsum3gsm
PubMed19499593
UniProtQ9KU37|NAGZ_VIBCH Beta-hexosaminidase (Gene Name=nagZ)

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