Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6H23

Crystal structure of the hClpP Y118A mutant with an activating small molecule

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	0006508	biological_process	proteolysis
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0006508	biological_process	proteolysis
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0006508	biological_process	proteolysis
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0004252	molecular_function	serine-type endopeptidase activity
F	0006508	biological_process	proteolysis
G	0004176	molecular_function	ATP-dependent peptidase activity
G	0004252	molecular_function	serine-type endopeptidase activity
G	0006508	biological_process	proteolysis
H	0004176	molecular_function	ATP-dependent peptidase activity
H	0004252	molecular_function	serine-type endopeptidase activity
H	0006508	biological_process	proteolysis
I	0004176	molecular_function	ATP-dependent peptidase activity
I	0004252	molecular_function	serine-type endopeptidase activity
I	0006508	biological_process	proteolysis
J	0004176	molecular_function	ATP-dependent peptidase activity
J	0004252	molecular_function	serine-type endopeptidase activity
J	0006508	biological_process	proteolysis
K	0004176	molecular_function	ATP-dependent peptidase activity
K	0004252	molecular_function	serine-type endopeptidase activity
K	0006508	biological_process	proteolysis
L	0004176	molecular_function	ATP-dependent peptidase activity
L	0004252	molecular_function	serine-type endopeptidase activity
L	0006508	biological_process	proteolysis
M	0004176	molecular_function	ATP-dependent peptidase activity
M	0004252	molecular_function	serine-type endopeptidase activity
M	0006508	biological_process	proteolysis
N	0004176	molecular_function	ATP-dependent peptidase activity
N	0004252	molecular_function	serine-type endopeptidase activity
N	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue FJT A 301

Chain	Residue
A	ALA101
B	VAL148
A	LEU104
A	PHE105
A	SER108
A	TYR138
B	LEU79
B	GLU82
B	ILE84
B	TRP146

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 302

Chain	Residue
A	GLN194
A	ALA195
H	GLN179
H	LYS202

site_id	AC3
Number of Residues	14
Details	binding site for residue FJT B 301

Chain	Residue
B	ILE100
B	ALA101
B	LEU104
B	PHE105
B	GLN107
B	SER108
B	THR135
B	TYR138
C	ARG78
C	LEU79
C	GLU82
C	ILE84
C	TRP146
C	VAL148

site_id	AC4
Number of Residues	11
Details	binding site for residue FJT D 301

Chain	Residue
C	ILE100
C	ALA101
C	LEU104
C	PHE105
C	SER108
C	TYR138
D	LEU79
D	GLU82
D	ILE84
D	TRP146
D	VAL148

site_id	AC5
Number of Residues	10
Details	binding site for residue FJT D 302

Chain	Residue
D	ILE100
D	ALA101
D	LEU104
D	PHE105
D	SER108
D	TYR138
E	ARG78
E	LEU79
E	GLU82
E	TRP146

site_id	AC6
Number of Residues	12
Details	binding site for residue FJT E 301

Chain	Residue
E	ILE100
E	ALA101
E	LEU104
E	PHE105
E	SER108
E	TYR138
F	ARG78
F	LEU79
F	GLU82
F	ILE84
F	TRP146
F	VAL148

site_id	AC7
Number of Residues	1
Details	binding site for residue EDO E 302

Chain	Residue
E	LYS202

site_id	AC8
Number of Residues	10
Details	binding site for residue FJT F 301

Chain	Residue
F	ALA101
F	LEU104
F	PHE105
F	SER108
F	TYR138
G	LEU79
G	GLU82
G	ILE84
G	TRP146
G	VAL148

site_id	AC9
Number of Residues	2
Details	binding site for residue EDO F 302

Chain	Residue
F	GLN179
F	ILE198

site_id	AD1
Number of Residues	10
Details	binding site for residue FJT G 301

Chain	Residue
A	LEU79
A	GLU82
A	ILE84
A	TRP146
G	ILE100
G	ALA101
G	LEU104
G	PHE105
G	SER108
G	TYR138

site_id	AD2
Number of Residues	11
Details	binding site for residue FJT H 301

Chain	Residue
H	ARG78
H	LEU79
H	GLU82
H	TRP146
H	VAL148
N	ILE100
N	ALA101
N	LEU104
N	PHE105
N	SER108
N	TYR138

site_id	AD3
Number of Residues	10
Details	binding site for residue FJT H 302

Chain	Residue
H	GLN107
H	SER108
H	TYR138
I	LEU79
I	GLU82
I	ILE84
H	ILE100
H	ALA101
H	LEU104
H	PHE105

site_id	AD4
Number of Residues	11
Details	binding site for residue FJT J 301

Chain	Residue
I	ILE100
I	ALA101
I	LEU104
I	PHE105
I	SER108
I	TYR138
J	ARG78
J	LEU79
J	GLU82
J	TRP146
J	VAL148

site_id	AD5
Number of Residues	13
Details	binding site for residue FJT K 301

Chain	Residue
J	ALA101
J	LEU104
J	PHE105
J	SER108
J	TYR138
K	ARG78
K	LEU79
K	GLU82
K	ILE84
K	HIS116
K	ALA118
K	TRP146
K	VAL148

site_id	AD6
Number of Residues	13
Details	binding site for residue FJT L 301

Chain	Residue
K	LEU104
K	PHE105
K	SER108
K	THR135
K	TYR138
L	ARG78
L	LEU79
L	GLU82
L	ILE84
L	ALA118
L	TRP146
L	VAL148
L	LEU170

site_id	AD7
Number of Residues	10
Details	binding site for residue FJT M 301

Chain	Residue
L	ILE100
L	LEU104
L	PHE105
L	GLN107
L	SER108
M	LEU79
M	GLU82
M	ILE84
M	TRP146
M	VAL148

site_id	AD8
Number of Residues	10
Details	binding site for residue FJT M 302

Chain	Residue
M	ALA101
M	LEU104
M	PHE105
M	SER108
M	TYR138
N	LEU79
N	GLU82
N	ILE84
N	TRP146
N	VAL148

site_id	AD9
Number of Residues	3
Details	binding site for residue EDO N 301

Chain	Residue
N	GLN179
N	ILE198
N	LYS202

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR145-SER156

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

Chain	Residue	Details
A	ARG167-PRO180

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11923310","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	14
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	14
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O88696","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	14
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)