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The structure of the caulobacter crescentus clps protease adaptor protein in complex with a N-end rule peptide

Analyse The structure of the caulobacter crescentus clps protease adaptor protein in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DNJ
Type
protein
Length
167 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent clp protease adapter protein clps; Synthetic N-end rule peptide
UniProt
Q9A5I0
Ligands
MG
Pockets
2 · best druggability 0.36

Structure

x-ray diffraction · 3 distinct chains · 52% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AATP-dependent clp protease adapter protein clpsprotein8054% helix, 24% strandQ9A5I0
BATP-dependent clp protease adapter protein clpsprotein8152% helix, 26% strandQ9A5I0
C, DSynthetic N-end rule peptideprotein30% helix, 33% strand—

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11200.360.7321empty
2560.260.7314empty

Interfaces

3 interfaces between chains.

  • A–B · 485 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 306 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 295 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 3DNJ · The structure of the Caulobacter crescentus ClpS protease adaptor protein in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9A5I0 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease adapter protein clps… · a predicted model of the same protein · chain A against A, TM-score 0.99

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