Structure of PDB 8e91 Chain C Binding Site BS02
Receptor Information
>8e91 Chain C (length=352) Species:
562
(Escherichia coli) [
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ALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGK
SNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENII
QKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALL
KLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRV
ETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVA
TLNELSEEALIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKA
MARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSEPLLI
YG
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
8e91 Chain C Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
8e91
Cryo-EM structure of substrate-free DNClpX.ClpP
Resolution
2.57 Å
Binding residue
(original residue number in PDB)
T126 D184
Binding residue
(residue number reindexed from 1)
T64 D122
Annotation score
1
Enzymatic activity
Enzyme Commision number
?
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:8e91
,
PDBe:8e91
,
PDBj:8e91
PDBsum
8e91
PubMed
UniProt
P0A6H1
|CLPX_ECOLI ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)
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