Structure of PDB 6vfx Chain C

Receptor sequence
>6vfxC (length=333) Species: 487 (Neisseria meningitidis) [Search protein sequence]
KLPTPAEIVANLNDHVIGQEQAKKALAVSVYNHYKRLRHPKAGANVELSK
SNILLIGPTGSGKTLLAQSLARKLDVPFVMADATTLTEAGYVGEDVEQII
TKLLGKCDFDVEKAQRGIVYIDQIDKISRTRDVSGEGVQQALLKLIEGTV
ASVPPQGGEFINVDTTNILFICGGAFAGLEKVIRQRTEKGGIGFGASVHN
ADITKLFGIVEPEDLIKFGLIPELIGRLPVIATLEILDEDALINILTEPK
NALVKQYQALFGMENVELEFEEGALRSIARQAMERKTGARGLRSIVERCL
LDTMYRLPDLKGLKKVVVGKAVIEEGREPELVF
3D structure
PDB6vfx A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
ChainC
Resolution2.9 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 peptide C Y153 V154 Y91 V92
BS02 ATP C V78 I79 G122 S123 G124 K125 T126 L127 I324 A368 R369 V16 I17 G60 S61 G62 K63 T64 L65 I245 A289 R290
BS03 MG C T126 D184 T64 D122
BS04 ATP C E302 R306 E223 R227
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
GO:0046983 protein dimerization activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0051301 cell division
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
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:6vfx, PDBe:6vfx, PDBj:6vfx
PDBsum6vfx
PubMed31916936
UniProtQ9JYY3|CLPX_NEIMB ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)

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