Structure of PDB 5utp Chain B

Receptor sequence
>5utpB (length=335) Species: 95486 (Burkholderia cenocepacia) [Search protein sequence]
KTTPGPVMLDVVGTTLSRDDARRLAHPNTGGVILFARHFQNRAQLTALTD
SIRAVREDILIAVDHEGGRVQRFRTDGFTVLPAMRRLGELWDRDVLLATK
VATAVGYILAAELRACGIDMSFTPVLDLDYGHSKVIGDRAFHRDPRVVTL
LAKSLNHGLSLAGMANCGKHFPGHGFAELPTDDRTLDAILEQDVAPYDWL
GLSLAAVIPAHVIYTQVDKRPAGFSRVWLQDILRGKLGFTGAIFSDDLSM
EAAREGGTLTQAADAALAAGCDMVLVCNQPDAAEVVLNGLKARASAESVR
RIKRMRARGKALKWDKLIAQPEYLQAQALLSSALA
3D structure
PDB5utp Conformational flexibility of the glycosidase NagZ allows it to bind structurally diverse inhibitors to suppress beta-lactam antibiotic resistance.
ChainB
Resolution2.2 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 8M7 B D65 R140 K170 H171 H175 D253 D254 M257 D64 R139 K169 H170 H174 D246 D247 M250 MOAD: Ki=3uM
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: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:5utp, PDBe:5utp, PDBj:5utp
PDBsum5utp
PubMed28370529
UniProtB4EA43

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