Structure of PDB 8e91 Chain C

Receptor sequence
>8e91C (length=352) Species: 562 (Escherichia coli) [Search protein sequence]
ALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGK
SNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENII
QKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALL
KLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRV
ETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVA
TLNELSEEALIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKA
MARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSEPLLI
YG
3D structure
PDB8e91 Cryo-EM structure of substrate-free DNClpX.ClpP
ChainC
Resolution2.57 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 AGS C Y77 V78 I79 G122 G124 K125 T126 L127 I325 A369 R370 Y15 V16 I17 G60 G62 K63 T64 L65 I263 A307 R308
BS02 MG C T126 D184 T64 D122
Gene Ontology
Molecular Function
GO:0002020 protease binding
GO:0004176 ATP-dependent peptidase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0046983 protein dimerization activity
GO:0051082 unfolded protein binding
GO:0097718 disordered domain specific binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0030164 protein denaturation
GO:0043335 protein unfolding
GO:0051301 cell division
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005829 cytosol
GO:0009368 endopeptidase Clp complex
GO:0009376 HslUV protease complex

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Cellular Component
External links
PDB RCSB:8e91, PDBe:8e91, PDBj:8e91
PDBsum8e91
PubMed
UniProtP0A6H1|CLPX_ECOLI ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)

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