Structure of PDB 3hln Chain I

Receptor sequence

>3hlnI (length=163) Species: 83333 (Escherichia coli K-12)

DIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIYLYINSPG
GVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGKRFCLPNS
RVMIHQPHCREILKVKGRMNELMALHTGQSLEQIERDTERDRFLSAPEAV
EYGLVDSILTHRN

3D structure

• PDB: 3hln Structural and Theoretical Studies Indicate that the Cylindrical Protease ClpP Samples Extended and Compact Conformations.
• Chain: I
• Resolution: 3.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G68 S97 M98 H122 D171
• Catalytic site (residue number reindexed from 1): G51 S80 M81 H105 D141
• 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	CA	I	E162 Q163	E132 Q133

Gene Ontology

Molecular Function

• GO:0004176 ATP-dependent peptidase activity
• GO:0004252 serine-type endopeptidase activity
• GO:0005515 protein binding
• 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:0009266 response to temperature stimulus
• GO:0009314 response to radiation
• GO:0009408 response to heat
• GO:0010498 proteasomal protein catabolic process
• GO:0043068 positive regulation of programmed cell death

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0009368 endopeptidase Clp complex
• GO:0009376 HslUV protease complex
• GO:0016020 membrane

External links

• PDB: RCSB:3hln, PDBe:3hln, PDBj:3hln
• PDBsum: 3hln
• PubMed: 20637416
• UniProt: P0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)