Structure of PDB 4jwk Chain A

Receptor sequence
>4jwkA (length=193) Species: 575584 (Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841) [Search protein sequence]
MSNISLIVGLGNPGSEYAQTRHNAGFWFVEQLADKYGITLKNDPKFHGIS
GRGNIEGHDVRLLLPMTYMNRSGQSVVPFSKFYQIAPEAILIAHDELDMN
PGVIRLKTGGGHGGHNGLRDIVPHIGPNFHRLRIGIGHPGSKERVSGHVL
GKAPSNEQSLMDGAIDHALSKVKLLVQGQVPQAMNQINAYKPA
3D structure
PDB4jwk The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii
ChainA
Resolution1.87 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 CTN A H22 Y68 M69 N70 N116 L150 H22 Y68 M69 N70 N116 L150 MOAD: Kd=5.3nM
PDBbind-CN: -logKd/Ki=8.32,Kd=4.79nM
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:4jwk, PDBe:4jwk, PDBj:4jwk
PDBsum4jwk
PubMed23844024
UniProtD0C9L6

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