Structure of PDB 5utr Chain A

Receptor sequence
>5utrA (length=339) Species: 95486 (Burkholderia cenocepacia) [Search protein sequence]
TTPGPVMLDVVGTTLSRDDARRLAHPNTGGVILFARHFQNRAQLTALTDS
IRAVREDILIAVDHEGGRVQRFRTDGFTVLPAMRRLGELWDRDVLLATKV
ATAVGYILAAELRACGIDMSFTPVLDLDYGHSKVIGDRAFHRDPRVVTLL
AKSLNHGLSLAGMANCGKHFPGHGFAEADSHVALPTDDRTLDAILEQDVA
PYDWLGLSLAAVIPAHVIYTQVDKRPAGFSRVWLQDILRGKLGFTGAIFS
DDLSMEAAREGGTLTQAADAALAAGCDMVLVCNQPDAAEVVLNGLKARAS
AESVRRIKRMRARGKALKWDKLIAQPEYLQAQALLSSAL
3D structure
PDB5utr Conformational flexibility of the glycosidase NagZ allows it to bind structurally diverse inhibitors to suppress beta-lactam antibiotic resistance.
ChainA
Resolution2.15 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 8MP A D65 V136 R140 K170 H171 S182 H183 D253 M257 D63 V134 R138 K168 H169 S180 H181 D251 M255 MOAD: Kd=7uM
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:5utr, PDBe:5utr, PDBj:5utr
PDBsum5utr
PubMed28370529
UniProtB4EA43

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