Structure of PDB 6vfs Chain A

Receptor sequence
>6vfsA (length=295) Species: 487 (Neisseria meningitidis) [Search protein sequence]
KLPTPAEIVANLNDHVIGQEQAKKALAVSVYNHYKRLRHLSKSNILLIGP
TGSGKTLLAQSLARKLDVPFVMADATTLDVEQIITKLLGKCDFDVEKAQR
GIVYIDQIDKISEGVQQALLKLIEGTVASVPNVDTTNILFICGGAFAGLE
KVIRQRTGGIGFGASTKLFGIVEPEDLIKFGLIPELIGRLPVIATLEILD
EDALINILTEPKNALVKQYQALFGMENVELEFEEGALRSIARQAMERKTG
ARGLRSIVERCLLDTMYRLPDLKGLKKVVVGKAVIEEGREPELVF
3D structure
PDB6vfs A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
ChainA
Resolution3.3 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 ADP A V78 I79 Q81 G122 S123 G124 T126 L127 I324 A368 R369 V16 I17 Q19 G52 S53 G54 T56 L57 I207 A251 R252
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6vfs, PDBe:6vfs, PDBj:6vfs
PDBsum6vfs
PubMed31916936
UniProtQ9JYY3|CLPX_NEIMB ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)

[Back to BioLiP]