Structure of PDB 1tg6 Chain G

Receptor sequence

>1tg6G (length=194) Species: 9606 (Homo sapiens)

PLIPIVVYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPI
HMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPG
MRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQ
SLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLV

3D structure

• PDB: 1tg6 Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP
• Chain: G
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G68 S97 M98 H122 D171
• Catalytic site (residue number reindexed from 1): G59 S88 M89 H113 D162
• Enzyme Commision number: 3.4.21.92: endopeptidase Clp.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FME	G	G67 G68 V70 S97 M98 H122 P124	G58 G59 V61 S88 M89 H113 P115

Gene Ontology

Molecular Function

• GO:0004175 endopeptidase activity
• GO:0004176 ATP-dependent peptidase activity
• GO:0004252 serine-type endopeptidase activity
• GO:0005515 protein binding
• GO:0008233 peptidase activity
• GO:0008236 serine-type peptidase activity
• GO:0042802 identical protein binding
• GO:0051117 ATPase binding

Biological Process

• GO:0006508 proteolysis
• GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
• GO:0033619 membrane protein proteolysis
• GO:0035694 mitochondrial protein catabolic process
• GO:0051603 proteolysis involved in protein catabolic process

Cellular Component

• GO:0005739 mitochondrion
• GO:0005759 mitochondrial matrix
• GO:0009368 endopeptidase Clp complex

External links

• PDB: RCSB:1tg6, PDBe:1tg6, PDBj:1tg6
• PDBsum: 1tg6
• PubMed: 15522782
• UniProt: Q16740|CLPP_HUMAN ATP-dependent Clp protease proteolytic subunit, mitochondrial (Gene Name=CLPP)