6HWM

Structure of Thermus thermophilus ClpP in complex with bortezomib

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004176	molecular_function	ATP-dependent peptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
A	0009368	cellular_component	endopeptidase Clp complex
A	0051117	molecular_function	ATPase binding
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
B	0009368	cellular_component	endopeptidase Clp complex
B	0051117	molecular_function	ATPase binding
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
C	0009368	cellular_component	endopeptidase Clp complex
C	0051117	molecular_function	ATPase binding
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005737	cellular_component	cytoplasm
D	0006508	biological_process	proteolysis
D	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
D	0009368	cellular_component	endopeptidase Clp complex
D	0051117	molecular_function	ATPase binding
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005737	cellular_component	cytoplasm
E	0006508	biological_process	proteolysis
E	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
E	0009368	cellular_component	endopeptidase Clp complex
E	0051117	molecular_function	ATPase binding
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0004252	molecular_function	serine-type endopeptidase activity
F	0005737	cellular_component	cytoplasm
F	0006508	biological_process	proteolysis
F	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
F	0009368	cellular_component	endopeptidase Clp complex
F	0051117	molecular_function	ATPase binding
G	0004176	molecular_function	ATP-dependent peptidase activity
G	0004252	molecular_function	serine-type endopeptidase activity
G	0005737	cellular_component	cytoplasm
G	0006508	biological_process	proteolysis
G	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
G	0009368	cellular_component	endopeptidase Clp complex
G	0051117	molecular_function	ATPase binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue BO2 A 301

Chain	Residue
A	GLY67
A	TRP125
A	ILE142
A	GLY68
A	GLU69
A	VAL70
A	SER97
A	MET98
A	HIS122
A	GLN123
A	PRO124

---

site_id	AC2
Number of Residues	2
Details	binding site for residue PEG C 302

Chain	Residue
C	GLY158
C	GLU181

---

site_id	AC3
Number of Residues	2
Details	binding site for residue PEG E 302

Chain	Residue
E	THR157
E	GLU181

---

site_id	AC4
Number of Residues	4
Details	binding site for residue PEG G 302

Chain	Residue
G	THR157
G	GLY158
G	LEU180
G	GLU181

---

site_id	AC5
Number of Residues	14
Details	binding site for Di-peptide BO2 B 301 and SER B 97

Chain	Residue
B	GLY67
B	GLY68
B	GLU69
B	VAL70
B	ALA96
B	MET98
B	ALA99
B	ALA100
B	VAL101
B	MET120
B	HIS122
B	GLN123
B	PRO124
B	TRP125

---

site_id	AC6
Number of Residues	14
Details	binding site for Di-peptide BO2 C 301 and SER C 97

Chain	Residue
C	GLY67
C	GLY68
C	GLU69
C	VAL70
C	ALA96
C	MET98
C	ALA99
C	ALA100
C	VAL101
C	MET120
C	HIS122
C	PRO124
C	TRP125
C	ILE142

---

site_id	AC7
Number of Residues	16
Details	binding site for Di-peptide BO2 D 301 and SER D 97

Chain	Residue
D	GLY67
D	GLY68
D	GLU69
D	VAL70
D	ALA96
D	MET98
D	ALA99
D	ALA100
D	VAL101
D	MET120
D	HIS122
D	GLN123
D	PRO124
D	TRP125
D	ILE142
D	LEU149

---

site_id	AC8
Number of Residues	16
Details	binding site for Di-peptide BO2 E 301 and SER E 97

Chain	Residue
E	GLY67
E	GLY68
E	GLU69
E	VAL70
E	ALA96
E	MET98
E	ALA99
E	ALA100
E	VAL101
E	MET120
E	HIS122
E	GLN123
E	PRO124
E	TRP125
E	ILE142
E	LEU149

---

site_id	AC9
Number of Residues	17
Details	binding site for Di-peptide BO2 F 301 and SER F 97

Chain	Residue
F	PRO66
F	GLY67
F	GLY68
F	GLU69
F	VAL70
F	ALA96
F	MET98
F	ALA99
F	ALA100
F	VAL101
F	MET120
F	HIS122
F	GLN123
F	PRO124
F	TRP125
F	ILE142
F	LEU149

---

site_id	AD1
Number of Residues	16
Details	binding site for Di-peptide BO2 G 301 and SER G 97

Chain	Residue
G	VAL70
G	ALA96
G	MET98
G	ALA99
G	ALA100
G	VAL101
G	MET120
G	HIS122
G	GLN123
G	PRO124
G	TRP125
G	ILE142
G	LEU149
G	GLY67
G	GLY68
G	GLU69

---

Functional Information from PROSITE/UniProt

site_id	PS00381
Number of Residues	12
Details	CLP_PROTEASE_SER Endopeptidase Clp serine active site. TivIGmAASMAA

Chain	Residue	Details
A	THR89-ALA100

---

site_id	PS00382
Number of Residues	14
Details	CLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RyalPhakVMIHQP

Chain	Residue	Details
A	ARG111-PRO124

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00444","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	7
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00444","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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