6J93

Crystal structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 0.95 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004045	molecular_function	aminoacyl-tRNA hydrolase activity
A	0005737	cellular_component	cytoplasm
A	0006412	biological_process	translation
A	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue EDO A 201

Chain	Residue
A	MET1
A	SER2
A	ASN3
A	ARG52
A	SER155
A	GLY178
A	HOH307
A	HOH422
A	HOH458

---

Functional Information from PROSITE/UniProt

site_id	PS01195
Number of Residues	14
Details	PEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YaqTRHNaGfwFVE

Chain	Residue	Details
A	TYR17-GLU30

---

site_id	PS01196
Number of Residues	11
Details	PEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLRDI

Chain	Residue	Details
A	GLY111-ILE121

---