Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7UVU

Crystal structure of human ClpP protease in complex with TR-107

Functional Information from GO Data
ChainGOidnamespacecontents
A0004176molecular_functionATP-dependent peptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004176molecular_functionATP-dependent peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004176molecular_functionATP-dependent peptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
D0004176molecular_functionATP-dependent peptidase activity
D0004252molecular_functionserine-type endopeptidase activity
D0006508biological_processproteolysis
E0004176molecular_functionATP-dependent peptidase activity
E0004252molecular_functionserine-type endopeptidase activity
E0006508biological_processproteolysis
F0004176molecular_functionATP-dependent peptidase activity
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004176molecular_functionATP-dependent peptidase activity
G0004252molecular_functionserine-type endopeptidase activity
G0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00381
Number of Residues12
DetailsCLP_PROTEASE_SER Endopeptidase Clp serine active site. TwcVGqAASMGS
ChainResidueDetails
ATHR145-SER156

site_idPS00382
Number of Residues14
DetailsCLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RhslPnsrIMIHQP
ChainResidueDetails
AARG167-PRO180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:11923310
ChainResidueDetails
ASER153
BSER153
CSER153
DSER153
ESER153
FSER153
GSER153

site_idSWS_FT_FI2
Number of Residues7
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS178
BHIS178
CHIS178
DHIS178
EHIS178
FHIS178
GHIS178

site_idSWS_FT_FI3
Number of Residues7
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O88696
ChainResidueDetails
ALYS200
BLYS200
CLYS200
DLYS200
ELYS200
FLYS200
GLYS200

site_idSWS_FT_FI4
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS211
BLYS211
CLYS211
DLYS211
ELYS211
FLYS211
GLYS211

219515

PDB entries from 2024-05-08

PDB statisticsPDBj update infoContact PDBjnumon