7BRD

Crystal structure of Peptidyl-tRNA hydrolase from Klebsiella pneumoniae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0003723	molecular_function	RNA binding
A	0004045	molecular_function	peptidyl-tRNA hydrolase activity
A	0005737	cellular_component	cytoplasm
A	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
A	0016787	molecular_function	hydrolase activity
A	0072344	biological_process	rescue of stalled ribosome
B	0000049	molecular_function	tRNA binding
B	0003723	molecular_function	RNA binding
B	0004045	molecular_function	peptidyl-tRNA hydrolase activity
B	0005737	cellular_component	cytoplasm
B	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
B	0016787	molecular_function	hydrolase activity
B	0072344	biological_process	rescue of stalled ribosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue PGE A 701

Chain	Residue
A	LYS44
A	ARG51
A	ARG60
A	TYR82

---

site_id	AC2
Number of Residues	3
Details	binding site for residue PEG A 702

Chain	Residue
A	ARG34
A	HIS35
A	LYS123

---

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 703

Chain	Residue
A	ASN126
A	HOH846
A	ARG51
A	ILE52

---

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 704

Chain	Residue
A	SER157
A	GLU158
A	ACT719
A	HOH806
A	HOH900
B	LYS73

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ACT A 705

Chain	Residue
A	GLU41
A	TYR48
A	HOH830
B	SER122

---

site_id	AC6
Number of Residues	5
Details	binding site for residue ACT A 706

Chain	Residue
A	GLY13
A	ALA14
A	GLU15
B	HIS111
B	HOH456

---

site_id	AC7
Number of Residues	3
Details	binding site for residue ACT A 707

Chain	Residue
A	LYS106
A	GLY109
A	GLY110

---

site_id	AC8
Number of Residues	3
Details	binding site for residue ACT A 708

Chain	Residue
A	GLN159
A	ASP163
A	HOH929

---

site_id	AC9
Number of Residues	2
Details	binding site for residue EDO A 709

Chain	Residue
A	LYS104
A	ARG134

---

site_id	AD1
Number of Residues	3
Details	binding site for residue EDO A 710

Chain	Residue
A	ALA156
A	HOH884
A	HOH930

---

site_id	AD2
Number of Residues	1
Details	binding site for residue ACT A 711

Chain	Residue
A	ARG20

---

site_id	AD3
Number of Residues	1
Details	binding site for residue ACT A 712

Chain	Residue
A	ARG34

---

site_id	AD4
Number of Residues	4
Details	binding site for residue CL A 713

Chain	Residue
A	ASN11
A	ASN115
B	ALA156
B	HOH493

---

site_id	AD5
Number of Residues	4
Details	binding site for residue CL A 714

Chain	Residue
A	LYS145
A	GLY148
B	LYS153
B	HOH516

---

site_id	AD6
Number of Residues	4
Details	binding site for residue CL A 715

Chain	Residue
A	ILE137
A	PHE149
A	GLU158
A	HOH927

---

site_id	AD7
Number of Residues	2
Details	binding site for residue CL A 716

Chain	Residue
A	GLU95
A	HOH889

---

site_id	AD8
Number of Residues	4
Details	binding site for residue SO4 A 717

Chain	Residue
A	ARG187
A	HOH802
B	ARG171
B	ARG187

---

site_id	AD9
Number of Residues	8
Details	binding site for residue SO4 A 718

Chain	Residue
A	GLU41
A	GLU42
A	SER43
A	ACT719
A	HOH808
A	HOH827
A	HOH857
A	HOH884

---

site_id	AE1
Number of Residues	2
Details	binding site for residue ACT A 719

Chain	Residue
A	EDO704
A	SO4718

---

site_id	AE2
Number of Residues	6
Details	binding site for residue PEG B 301

Chain	Residue
A	ASN129
A	HOH880
B	THR80
B	ARG83
B	HOH403
B	HOH429

---

site_id	AE3
Number of Residues	4
Details	binding site for residue EDO B 302

Chain	Residue
B	GLY110
B	HIS111
B	GLY112
B	HOH409

---

site_id	AE4
Number of Residues	2
Details	binding site for residue EDO B 303

Chain	Residue
B	LYS104
B	HIS189

---

site_id	AE5
Number of Residues	3
Details	binding site for residue EDO B 304

Chain	Residue
B	GLU41
B	SER43
B	LYS44

---

site_id	AE6
Number of Residues	4
Details	binding site for residue BME B 305

Chain	Residue
B	LYS106
B	GLY109
B	GLY110
B	HOH520

---

site_id	AE7
Number of Residues	5
Details	binding site for residue EDO B 306

Chain	Residue
B	LEU96
B	LEU98
B	PRO99
B	GLY138
B	HIS139

---

site_id	AE8
Number of Residues	2
Details	binding site for residue ACT B 307

Chain	Residue
B	LYS104
B	ARG134

---

site_id	AE9
Number of Residues	1
Details	binding site for residue ACT B 308

Chain	Residue
B	ASP29

---

site_id	AF1
Number of Residues	4
Details	binding site for residue SO4 B 309

Chain	Residue
B	ALA17
B	ALA18
B	ASN22
B	TRP26

---

site_id	AF2
Number of Residues	5
Details	binding site for residue SO4 B 310

Chain	Residue
B	LYS145
B	VAL146
B	VAL147
B	HOH489
A	GLN194

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TYR16-ASP29

---

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

Chain	Residue	Details
A	GLY110-ILE120

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Discriminates between blocked and unblocked aminoacyl-tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Stabilizes the basic form of H active site to accept a proton","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---