Structure of PDB 6vfs Chain C Binding Site BS03

Receptor Information

>6vfs Chain C (length=330) Species: 487 (Neisseria meningitidis)

KLPTPAEIVANLNDHVIGQEQAKKALAVSVYNHYKRLRHPKAGANVELSK
SNILLIGPTGSGKTLLAQSLARKLDVPFVMADATTLTEAGYVGEDVEQII
TKLLGKCDFDVEKAQRGIVYIDQIDKISRTRDVSGEGVQQALLKLIEGTV
ASVPPQEFINVDTTNILFICGGAFAGLEKVIRQRTEKGGIGFGASVHADI
TKLFGIVEPEDLIKFGLIPELIGRLPVIATLEILDEDALINILTEPKNAL
VKQYQALFGMENVELEFEEGALRSIARQAMERKTGARGLRSIVERCLLDT
MYRLPDLKGLKKVVVGKAVIEEGREPELVF

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 6vfs Chain C Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6vfs A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
• Resolution: 3.3 Å
• Binding residue (original residue number in PDB): T126 D184
• Binding residue (residue number reindexed from 1): T64 D122
• Annotation score: 1

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

External links

• PDB: RCSB:6vfs, PDBe:6vfs, PDBj:6vfs
• PDBsum: 6vfs
• PubMed: 31916936
• UniProt: Q9JYY3|CLPX_NEIMB ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)