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Structure of PDB 8et3 Chain A

Receptor sequence >8et3A (length=343) Species: 562 (Escherichia coli) [Search protein sequence] LPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNLGKSNILLIGPT GSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDY DVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAA VPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSGIGFG ATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEA LIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKAMARKTGARG LRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSEPLLIYG

3D structure PDB 8et3 The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery. Chain A Resolution 3.7 Å 3D structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

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 peptide A G152 Y153 V154 I198 T199 G81 Y82 V83 I127 T128 BS02 AGS A G122 S123 G124 K125 T126 L127 E185 I325 A369 R370 G51 S52 G53 K54 T55 L56 E114 I254 A298 R299

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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