Structure of PDB 4jx9 Chain A Binding Site BS01

Receptor Information
>4jx9 Chain A (length=193) Species: 575584 (Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSNISLIVGLGNPGSEYAQTRHNAGFWFVEQLADKYGITLKNDPKFHGIS
GRGNIEGHDVRLLLPMTYMNRSGQSVVPFSKFYQIAPEAILIAHDELDMN
PGVIRLKTGGGHGGHNGLRDIVPHIGPNFHRLRIGIGHPGSKERVSGHVL
GKAPSNEQSLMDGAIDHALSKVKLLVQGQVPQAMNQINAYKPA
Ligand information
Ligand IDURI
InChIInChI=1S/C9H12N2O6/c12-3-4-6(14)7(15)8(17-4)11-2-1-5(13)10-9(11)16/h1-2,4,6-8,12,14-15H,3H2,(H,10,13,16)/t4-,6-,7-,8-/m1/s1
InChIKeyDRTQHJPVMGBUCF-XVFCMESISA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC[CH]1O[CH]([CH](O)[CH]1O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.5.0C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO)O)O
ACDLabs 10.04O=C1NC(=O)N(C=C1)C2OC(C(O)C2O)CO
OpenEye OEToolkits 1.5.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)CO)O)O
CACTVS 3.341OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N2C=CC(=O)NC2=O
FormulaC9 H12 N2 O6
NameURIDINE
ChEMBLCHEMBL100259
DrugBankDB02745
ZINCZINC000002583633
PDB chain4jx9 Chain A Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4jx9 The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii
Resolution1.4 Å
Binding residue
(original residue number in PDB)		N12 Y17 H22 M69 N70 N116
Binding residue
(residue number reindexed from 1)		N12 Y17 H22 M69 N70 N116
Annotation score1
Binding affinityMOAD: Kd=1.4nM
PDBbind-CN: -logKd/Ki=8.62,Kd=2.4nM
Enzymatic activity
Catalytic site (original residue number in PDB) H22 N70 D95 N116
Catalytic site (residue number reindexed from 1) H22 N70 D95 N116
Enzyme Commision number 3.1.1.29: peptidyl-tRNA hydrolase.
Gene Ontology
Molecular Function
GO:0004045 aminoacyl-tRNA hydrolase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006412 translation
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:4jx9, PDBe:4jx9, PDBj:4jx9
PDBsum4jx9
PubMed23844024
UniProtD0C9L6

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