8HGK

Crystal structure of human ClpP in complex with ZK53

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 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

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

Chain	Residue	Details
A	ARG167-PRO180

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:11923310

Chain	Residue	Details
A	SER153
J	SER153
K	SER153
L	SER153
M	SER153
N	SER153
B	SER153
C	SER153
D	SER153
E	SER153
F	SER153
G	SER153
H	SER153
I	SER153

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	HIS178
J	HIS178
K	HIS178
L	HIS178
M	HIS178
N	HIS178
B	HIS178
C	HIS178
D	HIS178
E	HIS178
F	HIS178
G	HIS178
H	HIS178
I	HIS178

---

site_id	SWS_FT_FI3
Number of Residues	14
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O88696

Chain	Residue	Details
A	LYS200
J	LYS200
K	LYS200
L	LYS200
M	LYS200
N	LYS200
B	LYS200
C	LYS200
D	LYS200
E	LYS200
F	LYS200
G	LYS200
H	LYS200
I	LYS200

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site_id	SWS_FT_FI4
Number of Residues	14
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS211
J	LYS211
K	LYS211
L	LYS211
M	LYS211
N	LYS211
B	LYS211
C	LYS211
D	LYS211
E	LYS211
F	LYS211
G	LYS211
H	LYS211
I	LYS211

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